GenomeNet

Database: PDB
Entry: 3UZY
LinkDB: 3UZY
Original site: 3UZY 
HEADER    OXIDOREDUCTASE                          07-DEC-11   3UZY              
TITLE     CRYSTAL STRUCTURE OF 5BETA-REDUCTASE (AKR1D1) E120H MUTANT IN COMPLEX 
TITLE    2 WITH NADP+ AND 5BETA-DIHYDROTESTOSTERONE                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3-OXO-5-BETA-STEROID 4-DEHYDROGENASE;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ALDO-KETO REDUCTASE FAMILY 1 MEMBER D1, DELTA(4)-3-         
COMPND   5 KETOSTEROID 5-BETA-REDUCTASE, DELTA(4)-3-OXOSTEROID 5-BETA-REDUCTASE;
COMPND   6 EC: 1.3.1.3;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AKR1D1, SRD5B1;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C41(DE3);                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A-AKR1D1                             
KEYWDS    ALDO-KETO REDUCTASE, STEROID AND BILE ACID METABOLISM, CATALYTIC      
KEYWDS   2 TETRAD MUTANT, TIM BARREL, OXIDOREDUCTASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.CHEN,D.W.CHRISTIANSON,T.M.PENNING                                   
REVDAT   3   08-NOV-17 3UZY    1       REMARK                                   
REVDAT   2   27-JUN-12 3UZY    1       JRNL                                     
REVDAT   1   21-MAR-12 3UZY    0                                                
JRNL        AUTH   M.CHEN,J.E.DRURY,D.W.CHRISTIANSON,T.M.PENNING                
JRNL        TITL   CONVERSION OF HUMAN STEROID 5BETA-REDUCTASE (AKR1D1) INTO    
JRNL        TITL 2 3β-HYDROXYSTEROID DEHYDROGENASE BY SINGLE POINT         
JRNL        TITL 3 MUTATION E120H: EXAMPLE OF PERFECT ENZYME ENGINEERING.       
JRNL        REF    J.BIOL.CHEM.                  V. 287 16609 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22437839                                                     
JRNL        DOI    10.1074/JBC.M111.338780                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.83 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.5_2                                         
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.97                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.080                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 56863                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2892                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 42.9773 -  5.0508    0.82     2556   119  0.1406 0.1548        
REMARK   3     2  5.0508 -  4.0099    0.86     2577   125  0.1324 0.1443        
REMARK   3     3  4.0099 -  3.5033    0.88     2571   146  0.1460 0.1837        
REMARK   3     4  3.5033 -  3.1831    0.89     2574   137  0.1696 0.2006        
REMARK   3     5  3.1831 -  2.9550    0.90     2587   139  0.1787 0.2238        
REMARK   3     6  2.9550 -  2.7808    0.90     2613   150  0.1811 0.2320        
REMARK   3     7  2.7808 -  2.6416    0.91     2620   137  0.1804 0.2122        
REMARK   3     8  2.6416 -  2.5266    0.91     2619   153  0.1778 0.2508        
REMARK   3     9  2.5266 -  2.4294    0.91     2639   136  0.1760 0.2289        
REMARK   3    10  2.4294 -  2.3455    0.92     2638   144  0.1773 0.2231        
REMARK   3    11  2.3455 -  2.2722    0.91     2570   152  0.1857 0.2219        
REMARK   3    12  2.2722 -  2.2073    0.91     2632   142  0.1868 0.2421        
REMARK   3    13  2.2073 -  2.1491    0.92     2639   125  0.1851 0.2823        
REMARK   3    14  2.1491 -  2.0967    0.92     2590   153  0.1942 0.2384        
REMARK   3    15  2.0967 -  2.0491    0.92     2652   111  0.1911 0.2760        
REMARK   3    16  2.0491 -  2.0054    0.91     2559   152  0.1871 0.2479        
REMARK   3    17  2.0054 -  1.9653    0.90     2582   150  0.1925 0.2334        
REMARK   3    18  1.9653 -  1.9282    0.89     2513   127  0.1892 0.2620        
REMARK   3    19  1.9282 -  1.8938    0.88     2553   130  0.1995 0.2747        
REMARK   3    20  1.8938 -  1.8617    0.86     2396   142  0.2028 0.2853        
REMARK   3    21  1.8617 -  1.8317    0.80     2291   122  0.2073 0.2534        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 30.27                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.480           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.96600                                              
REMARK   3    B22 (A**2) : -0.86200                                             
REMARK   3    B33 (A**2) : -0.04330                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           5615                                  
REMARK   3   ANGLE     :  1.117           7664                                  
REMARK   3   CHIRALITY :  0.070            835                                  
REMARK   3   PLANARITY :  0.006            975                                  
REMARK   3   DIHEDRAL  : 19.652           2204                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3UZY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000069420.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : CRYO-COOLED DOUBLE CRYSTAL         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58578                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.830                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 3UZW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 14-20% POLYETHYLENE      
REMARK 280  GLYCOL 4000, 10% ISOPROPANOL, PH 7.5, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.00750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.74850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.11200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.74850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.00750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.11200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A   8       33.70   -140.85                                   
REMARK 500    HIS A 197      174.81    178.35                                   
REMARK 500    THR A 224      169.39     73.39                                   
REMARK 500    TRP A 230       -7.87   -143.26                                   
REMARK 500    THR B 224      171.56     75.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BDT A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BDT B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 601                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UZW   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH NADP+ ONLY                           
REMARK 900 RELATED ID: 3UZX   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH NADP+ AND EPIANDROSTERONE            
REMARK 900 RELATED ID: 3UZZ   RELATED DB: PDB                                   
DBREF  3UZY A    1   326  UNP    P51857   AK1D1_HUMAN      1    326             
DBREF  3UZY B    1   326  UNP    P51857   AK1D1_HUMAN      1    326             
SEQADV 3UZY MET A  -19  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY GLY A  -18  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY SER A  -17  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY SER A  -16  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS A  -15  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS A  -14  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS A  -13  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS A  -12  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS A  -11  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS A  -10  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY SER A   -9  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY SER A   -8  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY GLY A   -7  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY LEU A   -6  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY VAL A   -5  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY PRO A   -4  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY ARG A   -3  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY GLY A   -2  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY SER A   -1  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS A    0  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS A  120  UNP  P51857    GLU   120 ENGINEERED MUTATION            
SEQADV 3UZY MET B  -19  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY GLY B  -18  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY SER B  -17  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY SER B  -16  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS B  -15  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS B  -14  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS B  -13  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS B  -12  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS B  -11  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS B  -10  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY SER B   -9  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY SER B   -8  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY GLY B   -7  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY LEU B   -6  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY VAL B   -5  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY PRO B   -4  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY ARG B   -3  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY GLY B   -2  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY SER B   -1  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS B    0  UNP  P51857              EXPRESSION TAG                 
SEQADV 3UZY HIS B  120  UNP  P51857    GLU   120 ENGINEERED MUTATION            
SEQRES   1 A  346  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  346  LEU VAL PRO ARG GLY SER HIS MET ASP LEU SER ALA ALA          
SEQRES   3 A  346  SER HIS ARG ILE PRO LEU SER ASP GLY ASN SER ILE PRO          
SEQRES   4 A  346  ILE ILE GLY LEU GLY THR TYR SER GLU PRO LYS SER THR          
SEQRES   5 A  346  PRO LYS GLY ALA CYS ALA THR SER VAL LYS VAL ALA ILE          
SEQRES   6 A  346  ASP THR GLY TYR ARG HIS ILE ASP GLY ALA TYR ILE TYR          
SEQRES   7 A  346  GLN ASN GLU HIS GLU VAL GLY GLU ALA ILE ARG GLU LYS          
SEQRES   8 A  346  ILE ALA GLU GLY LYS VAL ARG ARG GLU ASP ILE PHE TYR          
SEQRES   9 A  346  CYS GLY LYS LEU TRP ALA THR ASN HIS VAL PRO GLU MET          
SEQRES  10 A  346  VAL ARG PRO THR LEU GLU ARG THR LEU ARG VAL LEU GLN          
SEQRES  11 A  346  LEU ASP TYR VAL ASP LEU TYR ILE ILE HIS VAL PRO MET          
SEQRES  12 A  346  ALA PHE LYS PRO GLY ASP GLU ILE TYR PRO ARG ASP GLU          
SEQRES  13 A  346  ASN GLY LYS TRP LEU TYR HIS LYS SER ASN LEU CYS ALA          
SEQRES  14 A  346  THR TRP GLU ALA MET GLU ALA CYS LYS ASP ALA GLY LEU          
SEQRES  15 A  346  VAL LYS SER LEU GLY VAL SER ASN PHE ASN ARG ARG GLN          
SEQRES  16 A  346  LEU GLU LEU ILE LEU ASN LYS PRO GLY LEU LYS HIS LYS          
SEQRES  17 A  346  PRO VAL SER ASN GLN VAL GLU CYS HIS PRO TYR PHE THR          
SEQRES  18 A  346  GLN PRO LYS LEU LEU LYS PHE CYS GLN GLN HIS ASP ILE          
SEQRES  19 A  346  VAL ILE THR ALA TYR SER PRO LEU GLY THR SER ARG ASN          
SEQRES  20 A  346  PRO ILE TRP VAL ASN VAL SER SER PRO PRO LEU LEU LYS          
SEQRES  21 A  346  ASP ALA LEU LEU ASN SER LEU GLY LYS ARG TYR ASN LYS          
SEQRES  22 A  346  THR ALA ALA GLN ILE VAL LEU ARG PHE ASN ILE GLN ARG          
SEQRES  23 A  346  GLY VAL VAL VAL ILE PRO LYS SER PHE ASN LEU GLU ARG          
SEQRES  24 A  346  ILE LYS GLU ASN PHE GLN ILE PHE ASP PHE SER LEU THR          
SEQRES  25 A  346  GLU GLU GLU MET LYS ASP ILE GLU ALA LEU ASN LYS ASN          
SEQRES  26 A  346  VAL ARG PHE VAL GLU LEU LEU MET TRP ARG ASP HIS PRO          
SEQRES  27 A  346  GLU TYR PRO PHE HIS ASP GLU TYR                              
SEQRES   1 B  346  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  346  LEU VAL PRO ARG GLY SER HIS MET ASP LEU SER ALA ALA          
SEQRES   3 B  346  SER HIS ARG ILE PRO LEU SER ASP GLY ASN SER ILE PRO          
SEQRES   4 B  346  ILE ILE GLY LEU GLY THR TYR SER GLU PRO LYS SER THR          
SEQRES   5 B  346  PRO LYS GLY ALA CYS ALA THR SER VAL LYS VAL ALA ILE          
SEQRES   6 B  346  ASP THR GLY TYR ARG HIS ILE ASP GLY ALA TYR ILE TYR          
SEQRES   7 B  346  GLN ASN GLU HIS GLU VAL GLY GLU ALA ILE ARG GLU LYS          
SEQRES   8 B  346  ILE ALA GLU GLY LYS VAL ARG ARG GLU ASP ILE PHE TYR          
SEQRES   9 B  346  CYS GLY LYS LEU TRP ALA THR ASN HIS VAL PRO GLU MET          
SEQRES  10 B  346  VAL ARG PRO THR LEU GLU ARG THR LEU ARG VAL LEU GLN          
SEQRES  11 B  346  LEU ASP TYR VAL ASP LEU TYR ILE ILE HIS VAL PRO MET          
SEQRES  12 B  346  ALA PHE LYS PRO GLY ASP GLU ILE TYR PRO ARG ASP GLU          
SEQRES  13 B  346  ASN GLY LYS TRP LEU TYR HIS LYS SER ASN LEU CYS ALA          
SEQRES  14 B  346  THR TRP GLU ALA MET GLU ALA CYS LYS ASP ALA GLY LEU          
SEQRES  15 B  346  VAL LYS SER LEU GLY VAL SER ASN PHE ASN ARG ARG GLN          
SEQRES  16 B  346  LEU GLU LEU ILE LEU ASN LYS PRO GLY LEU LYS HIS LYS          
SEQRES  17 B  346  PRO VAL SER ASN GLN VAL GLU CYS HIS PRO TYR PHE THR          
SEQRES  18 B  346  GLN PRO LYS LEU LEU LYS PHE CYS GLN GLN HIS ASP ILE          
SEQRES  19 B  346  VAL ILE THR ALA TYR SER PRO LEU GLY THR SER ARG ASN          
SEQRES  20 B  346  PRO ILE TRP VAL ASN VAL SER SER PRO PRO LEU LEU LYS          
SEQRES  21 B  346  ASP ALA LEU LEU ASN SER LEU GLY LYS ARG TYR ASN LYS          
SEQRES  22 B  346  THR ALA ALA GLN ILE VAL LEU ARG PHE ASN ILE GLN ARG          
SEQRES  23 B  346  GLY VAL VAL VAL ILE PRO LYS SER PHE ASN LEU GLU ARG          
SEQRES  24 B  346  ILE LYS GLU ASN PHE GLN ILE PHE ASP PHE SER LEU THR          
SEQRES  25 B  346  GLU GLU GLU MET LYS ASP ILE GLU ALA LEU ASN LYS ASN          
SEQRES  26 B  346  VAL ARG PHE VAL GLU LEU LEU MET TRP ARG ASP HIS PRO          
SEQRES  27 B  346  GLU TYR PRO PHE HIS ASP GLU TYR                              
HET    NAP  A 401      48                                                       
HET    BDT  A 501      21                                                       
HET     CL  A 601       1                                                       
HET    NAP  B 401      48                                                       
HET    BDT  B 501      21                                                       
HET     CL  B 601       1                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     BDT 5-BETA-DIHYDROTESTOSTERONE                                       
HETNAM      CL CHLORIDE ION                                                     
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
HETSYN     BDT (5BETA,8ALPHA,17BETA)-17-HYDROXYANDROSTAN-3-ONE                  
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   4  BDT    2(C19 H30 O2)                                                
FORMUL   5   CL    2(CL 1-)                                                     
FORMUL   9  HOH   *550(H2 O)                                                    
HELIX    1   1 GLY A   35  GLY A   48  1                                  14    
HELIX    2   2 ALA A   55  GLN A   59  5                                   5    
HELIX    3   3 ASN A   60  GLU A   74  1                                  15    
HELIX    4   4 ARG A   78  ILE A   82  5                                   5    
HELIX    5   5 TRP A   89  HIS A   93  5                                   5    
HELIX    6   6 VAL A   94  GLU A   96  5                                   3    
HELIX    7   7 MET A   97  GLN A  110  1                                  14    
HELIX    8   8 ASN A  146  ALA A  160  1                                  15    
HELIX    9   9 ASN A  172  ASN A  181  1                                  10    
HELIX   10  10 GLN A  202  HIS A  212  1                                  11    
HELIX   11  11 PRO A  237  LYS A  240  5                                   4    
HELIX   12  12 ASP A  241  ASN A  252  1                                  12    
HELIX   13  13 THR A  254  ARG A  266  1                                  13    
HELIX   14  14 ASN A  276  GLN A  285  1                                  10    
HELIX   15  15 THR A  292  ALA A  301  1                                  10    
HELIX   16  16 LEU A  311  ARG A  315  5                                   5    
HELIX   17  17 GLY B   35  GLY B   48  1                                  14    
HELIX   18  18 ALA B   55  GLN B   59  5                                   5    
HELIX   19  19 ASN B   60  GLU B   74  1                                  15    
HELIX   20  20 ARG B   78  ILE B   82  5                                   5    
HELIX   21  21 TRP B   89  HIS B   93  5                                   5    
HELIX   22  22 VAL B   94  GLN B  110  1                                  17    
HELIX   23  23 ASN B  146  ALA B  160  1                                  15    
HELIX   24  24 ASN B  172  ASN B  181  1                                  10    
HELIX   25  25 GLN B  202  HIS B  212  1                                  11    
HELIX   26  26 PRO B  237  LYS B  240  5                                   4    
HELIX   27  27 ASP B  241  TYR B  251  1                                  11    
HELIX   28  28 THR B  254  ARG B  266  1                                  13    
HELIX   29  29 ASN B  276  GLN B  285  1                                  10    
HELIX   30  30 THR B  292  ALA B  301  1                                  10    
HELIX   31  31 LEU B  311  ARG B  315  5                                   5    
SHEET    1   A 2 ARG A   9  PRO A  11  0                                        
SHEET    2   A 2 SER A  17  PRO A  19 -1  O  ILE A  18   N  ILE A  10           
SHEET    1   B 8 LEU A  23  GLY A  24  0                                        
SHEET    2   B 8 HIS A  51  ASP A  53  1  O  ASP A  53   N  LEU A  23           
SHEET    3   B 8 PHE A  83  LEU A  88  1  O  PHE A  83   N  ILE A  52           
SHEET    4   B 8 VAL A 114  ILE A 119  1  O  ILE A 118   N  LEU A  88           
SHEET    5   B 8 VAL A 163  SER A 169  1  O  GLY A 167   N  TYR A 117           
SHEET    6   B 8 SER A 191  GLU A 195  1  O  SER A 191   N  VAL A 168           
SHEET    7   B 8 VAL A 215  TYR A 219  1  O  TYR A 219   N  VAL A 194           
SHEET    8   B 8 VAL A 269  VAL A 270  1  O  VAL A 269   N  ALA A 218           
SHEET    1   C 2 ARG B   9  PRO B  11  0                                        
SHEET    2   C 2 SER B  17  PRO B  19 -1  O  ILE B  18   N  ILE B  10           
SHEET    1   D 8 LEU B  23  GLY B  24  0                                        
SHEET    2   D 8 HIS B  51  ASP B  53  1  O  ASP B  53   N  LEU B  23           
SHEET    3   D 8 PHE B  83  LEU B  88  1  O  PHE B  83   N  ILE B  52           
SHEET    4   D 8 VAL B 114  ILE B 119  1  O  LEU B 116   N  GLY B  86           
SHEET    5   D 8 VAL B 163  SER B 169  1  O  GLY B 167   N  TYR B 117           
SHEET    6   D 8 SER B 191  GLU B 195  1  O  SER B 191   N  VAL B 168           
SHEET    7   D 8 VAL B 215  TYR B 219  1  O  TYR B 219   N  VAL B 194           
SHEET    8   D 8 VAL B 269  VAL B 270  1  O  VAL B 269   N  ALA B 218           
SITE     1 AC1 32 GLY A  24  THR A  25  TYR A  26  ASP A  53                    
SITE     2 AC1 32 TYR A  58  HIS A 120  SER A 169  ASN A 170                    
SITE     3 AC1 32 GLN A 193  TYR A 219  SER A 220  PRO A 221                    
SITE     4 AC1 32 LEU A 222  GLY A 223  THR A 224  SER A 225                    
SITE     5 AC1 32 LEU A 239  ALA A 256  ILE A 271  PRO A 272                    
SITE     6 AC1 32 LYS A 273  SER A 274  PHE A 275  ARG A 279                    
SITE     7 AC1 32 GLU A 282  ASN A 283  HOH A1042  HOH A1054                    
SITE     8 AC1 32 HOH A1079  HOH A1109  HOH A1131  HOH A1172                    
SITE     1 AC2  9 TYR A  26  ILE A  57  TYR A  58  HIS A 120                    
SITE     2 AC2  9 TYR A 132  TRP A 230  LEU A 311  TRP A 314                    
SITE     3 AC2  9 HOH A1230                                                     
SITE     1 AC3  6 LYS A  87  TRP A  89  THR A 101  ARG A 104                    
SITE     2 AC3  6 HOH A1010  HOH A1068                                          
SITE     1 AC4 35 GLY B  24  THR B  25  TYR B  26  ASP B  53                    
SITE     2 AC4 35 TYR B  58  HIS B 120  SER B 169  ASN B 170                    
SITE     3 AC4 35 GLN B 193  TYR B 219  SER B 220  PRO B 221                    
SITE     4 AC4 35 LEU B 222  GLY B 223  THR B 224  SER B 225                    
SITE     5 AC4 35 LEU B 239  ALA B 256  ILE B 271  PRO B 272                    
SITE     6 AC4 35 LYS B 273  SER B 274  PHE B 275  ARG B 279                    
SITE     7 AC4 35 GLU B 282  ASN B 283  HOH B1039  HOH B1057                    
SITE     8 AC4 35 HOH B1079  HOH B1094  HOH B1136  HOH B1169                    
SITE     9 AC4 35 HOH B1188  HOH B1243  HOH B1297                               
SITE     1 AC5  7 TYR B  26  ILE B  57  TYR B  58  HIS B 120                    
SITE     2 AC5  7 TRP B 230  MET B 313  HOH B1313                               
SITE     1 AC6  6 LYS B  87  TRP B  89  ASN B  92  THR B 101                    
SITE     2 AC6  6 ARG B 104  HOH B1009                                          
CRYST1   50.015  110.224  129.497  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019994  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009072  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007722        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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