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Database: PDB
Entry: 3BV7
LinkDB: 3BV7
Original site: 3BV7 
HEADER    OXIDOREDUCTASE                          04-JAN-08   3BV7              
TITLE     CRYSTAL STRUCTURE OF DELTA(4)-3-KETOSTEROID 5-BETA-REDUCTASE IN       
TITLE    2 COMPLEX WITH NADP AND GLYCEROL. RESOLUTION: 1.79 A.                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3-OXO-5-BETA-STEROID 4-DEHYDROGENASE;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DELTA(4)-3-KETOSTEROID 5-BETA-REDUCTASE, ALDO-KETO REDUCTASE
COMPND   5 FAMILY 1 MEMBER D1;                                                  
COMPND   6 EC: 1.3.1.3;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: LIVER;                                                        
SOURCE   6 GENE: AKR1D1, SRD5B1;                                                
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET28A;                               
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A-AKR1D1                             
KEYWDS    5-BETA-REDUCTASE; GLYCEROL; AKR1A1, BILE ACID CATABOLISM, DISEASE     
KEYWDS   2 MUTATION, LIPID METABOLISM, NADP, OXIDOREDUCTASE, STEROID METABOLISM 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.DI COSTANZO,J.DRURY,T.M.PENNING,D.W.CHRISTIANSON                    
REVDAT   5   24-JUL-19 3BV7    1       REMARK                                   
REVDAT   4   13-JUL-11 3BV7    1       VERSN                                    
REVDAT   3   24-FEB-09 3BV7    1       VERSN                                    
REVDAT   2   24-JUN-08 3BV7    1       JRNL                                     
REVDAT   1   01-APR-08 3BV7    0                                                
JRNL        AUTH   L.DI COSTANZO,J.E.DRURY,T.M.PENNING,D.W.CHRISTIANSON         
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN LIVER {DELTA}4-3-KETOSTEROID      
JRNL        TITL 2 5{BETA}-REDUCTASE (AKR1D1) AND IMPLICATIONS FOR SUBSTRATE    
JRNL        TITL 3 BINDING AND CATALYSIS.                                       
JRNL        REF    J.BIOL.CHEM.                  V. 283 16830 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18407998                                                     
JRNL        DOI    10.1074/JBC.M801778200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   CROSS-VALIDATION METHOD           : NULL                           
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.236                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.236                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.257                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2800                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 63320                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 5254                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 114                                           
REMARK   3   SOLVENT ATOMS      : 348                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL                    
REMARK   3   NUMBER OF RESTRAINTS                     : NULL                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.020                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.012                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.024                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL                    
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.031                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : NULL                                
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3BV7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000045996.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-NOV-07                          
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                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : ROSENBAUM-ROCK MONOCHROMATOR       
REMARK 200                                   HIGH-RESOLUTION DOUBLE-CRYSTAL     
REMARK 200                                   SI (111) SAGITTAL FOCUSING.        
REMARK 200                                   ROSENBAUM-ROCK VERTICAL FOCUSING   
REMARK 200                                   MIRROR.                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66774                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.10900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
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: 3BUR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 5.0 MG/ML AKR1D1, 2.0 MM        
REMARK 280  NADPH, 2.0 MM 5-BETA-CHOLESTAN-3-ONE, 10.0 MM TRIS (PH 7.4).        
REMARK 280  PRECIPITANT BUFFER: 0.1 M TRIS (PH 7.0), 10-20% (WT/VOL) PEG        
REMARK 280  4000, 10% ISOPROPANOL., PH 7.5, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  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       24.91300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.59300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.91650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.59300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.91300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.91650            
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     1                                                      
REMARK 465     MET B     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR B 326   C     TYR B 326   OXT     0.238                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TYR A  49   CA  -  CB  -  CG  ANGL. DEV. =  11.6 DEGREES          
REMARK 500    TYR A 219   CA  -  CB  -  CG  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    ARG B   9   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 107   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    PRO B 183   O   -  C   -  N   ANGL. DEV. = -10.6 DEGREES          
REMARK 500    TYR B 219   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    ARG B 266   CD  -  NE  -  CZ  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ARG B 266   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B 266   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG B 307   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG B 307   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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       34.94   -145.13                                   
REMARK 500    SER A 220       51.98     39.12                                   
REMARK 500    THR A 224      171.39     78.46                                   
REMARK 500    ASN A 232       82.88    -68.09                                   
REMARK 500    HIS B   8       40.10   -143.43                                   
REMARK 500    ASN B 146       79.04   -150.22                                   
REMARK 500    PHE B 200       74.93   -156.17                                   
REMARK 500    SER B 220       53.43     36.62                                   
REMARK 500    THR B 224      169.40     81.50                                   
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 3901                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 3902                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3991                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3992                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3999                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3BUR   RELATED DB: PDB                                   
REMARK 900 SAME ENZYME IN COMPLEX WITH NADP AND TESTOSTERONE                    
REMARK 900 RELATED ID: 3BUV   RELATED DB: PDB                                   
DBREF  3BV7 A    1   326  UNP    P51857   AK1D1_HUMAN      1    326             
DBREF  3BV7 B    1   326  UNP    P51857   AK1D1_HUMAN      1    326             
SEQRES   1 A  326  MET ASP LEU SER ALA ALA SER HIS ARG ILE PRO LEU SER          
SEQRES   2 A  326  ASP GLY ASN SER ILE PRO ILE ILE GLY LEU GLY THR TYR          
SEQRES   3 A  326  SER GLU PRO LYS SER THR PRO LYS GLY ALA CYS ALA THR          
SEQRES   4 A  326  SER VAL LYS VAL ALA ILE ASP THR GLY TYR ARG HIS ILE          
SEQRES   5 A  326  ASP GLY ALA TYR ILE TYR GLN ASN GLU HIS GLU VAL GLY          
SEQRES   6 A  326  GLU ALA ILE ARG GLU LYS ILE ALA GLU GLY LYS VAL ARG          
SEQRES   7 A  326  ARG GLU ASP ILE PHE TYR CYS GLY LYS LEU TRP ALA THR          
SEQRES   8 A  326  ASN HIS VAL PRO GLU MET VAL ARG PRO THR LEU GLU ARG          
SEQRES   9 A  326  THR LEU ARG VAL LEU GLN LEU ASP TYR VAL ASP LEU TYR          
SEQRES  10 A  326  ILE ILE GLU VAL PRO MET ALA PHE LYS PRO GLY ASP GLU          
SEQRES  11 A  326  ILE TYR PRO ARG ASP GLU ASN GLY LYS TRP LEU TYR HIS          
SEQRES  12 A  326  LYS SER ASN LEU CYS ALA THR TRP GLU ALA MET GLU ALA          
SEQRES  13 A  326  CYS LYS ASP ALA GLY LEU VAL LYS SER LEU GLY VAL SER          
SEQRES  14 A  326  ASN PHE ASN ARG ARG GLN LEU GLU LEU ILE LEU ASN LYS          
SEQRES  15 A  326  PRO GLY LEU LYS HIS LYS PRO VAL SER ASN GLN VAL GLU          
SEQRES  16 A  326  CYS HIS PRO TYR PHE THR GLN PRO LYS LEU LEU LYS PHE          
SEQRES  17 A  326  CYS GLN GLN HIS ASP ILE VAL ILE THR ALA TYR SER PRO          
SEQRES  18 A  326  LEU GLY THR SER ARG ASN PRO ILE TRP VAL ASN VAL SER          
SEQRES  19 A  326  SER PRO PRO LEU LEU LYS ASP ALA LEU LEU ASN SER LEU          
SEQRES  20 A  326  GLY LYS ARG TYR ASN LYS THR ALA ALA GLN ILE VAL LEU          
SEQRES  21 A  326  ARG PHE ASN ILE GLN ARG GLY VAL VAL VAL ILE PRO LYS          
SEQRES  22 A  326  SER PHE ASN LEU GLU ARG ILE LYS GLU ASN PHE GLN ILE          
SEQRES  23 A  326  PHE ASP PHE SER LEU THR GLU GLU GLU MET LYS ASP ILE          
SEQRES  24 A  326  GLU ALA LEU ASN LYS ASN VAL ARG PHE VAL GLU LEU LEU          
SEQRES  25 A  326  MET TRP ARG ASP HIS PRO GLU TYR PRO PHE HIS ASP GLU          
SEQRES  26 A  326  TYR                                                          
SEQRES   1 B  326  MET ASP LEU SER ALA ALA SER HIS ARG ILE PRO LEU SER          
SEQRES   2 B  326  ASP GLY ASN SER ILE PRO ILE ILE GLY LEU GLY THR TYR          
SEQRES   3 B  326  SER GLU PRO LYS SER THR PRO LYS GLY ALA CYS ALA THR          
SEQRES   4 B  326  SER VAL LYS VAL ALA ILE ASP THR GLY TYR ARG HIS ILE          
SEQRES   5 B  326  ASP GLY ALA TYR ILE TYR GLN ASN GLU HIS GLU VAL GLY          
SEQRES   6 B  326  GLU ALA ILE ARG GLU LYS ILE ALA GLU GLY LYS VAL ARG          
SEQRES   7 B  326  ARG GLU ASP ILE PHE TYR CYS GLY LYS LEU TRP ALA THR          
SEQRES   8 B  326  ASN HIS VAL PRO GLU MET VAL ARG PRO THR LEU GLU ARG          
SEQRES   9 B  326  THR LEU ARG VAL LEU GLN LEU ASP TYR VAL ASP LEU TYR          
SEQRES  10 B  326  ILE ILE GLU VAL PRO MET ALA PHE LYS PRO GLY ASP GLU          
SEQRES  11 B  326  ILE TYR PRO ARG ASP GLU ASN GLY LYS TRP LEU TYR HIS          
SEQRES  12 B  326  LYS SER ASN LEU CYS ALA THR TRP GLU ALA MET GLU ALA          
SEQRES  13 B  326  CYS LYS ASP ALA GLY LEU VAL LYS SER LEU GLY VAL SER          
SEQRES  14 B  326  ASN PHE ASN ARG ARG GLN LEU GLU LEU ILE LEU ASN LYS          
SEQRES  15 B  326  PRO GLY LEU LYS HIS LYS PRO VAL SER ASN GLN VAL GLU          
SEQRES  16 B  326  CYS HIS PRO TYR PHE THR GLN PRO LYS LEU LEU LYS PHE          
SEQRES  17 B  326  CYS GLN GLN HIS ASP ILE VAL ILE THR ALA TYR SER PRO          
SEQRES  18 B  326  LEU GLY THR SER ARG ASN PRO ILE TRP VAL ASN VAL SER          
SEQRES  19 B  326  SER PRO PRO LEU LEU LYS ASP ALA LEU LEU ASN SER LEU          
SEQRES  20 B  326  GLY LYS ARG TYR ASN LYS THR ALA ALA GLN ILE VAL LEU          
SEQRES  21 B  326  ARG PHE ASN ILE GLN ARG GLY VAL VAL VAL ILE PRO LYS          
SEQRES  22 B  326  SER PHE ASN LEU GLU ARG ILE LYS GLU ASN PHE GLN ILE          
SEQRES  23 B  326  PHE ASP PHE SER LEU THR GLU GLU GLU MET LYS ASP ILE          
SEQRES  24 B  326  GLU ALA LEU ASN LYS ASN VAL ARG PHE VAL GLU LEU LEU          
SEQRES  25 B  326  MET TRP ARG ASP HIS PRO GLU TYR PRO PHE HIS ASP GLU          
SEQRES  26 B  326  TYR                                                          
HET    NAP  A3901      48                                                       
HET    GOL  A3991       6                                                       
HET    GOL  A3992       6                                                       
HET    GOL  A3999       6                                                       
HET    NAP  B3902      48                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     GOL GLYCEROL                                                         
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   8  HOH   *348(H2 O)                                                    
HELIX    1   1 GLU A   28  THR A   32  5                                   5    
HELIX    2   2 GLY A   35  GLY A   48  1                                  14    
HELIX    3   3 ALA A   55  GLN A   59  5                                   5    
HELIX    4   4 ASN A   60  GLU A   74  1                                  15    
HELIX    5   5 ARG A   78  ILE A   82  5                                   5    
HELIX    6   6 TRP A   89  HIS A   93  5                                   5    
HELIX    7   7 VAL A   94  GLU A   96  5                                   3    
HELIX    8   8 MET A   97  GLN A  110  1                                  14    
HELIX    9   9 ASN A  146  ALA A  160  1                                  15    
HELIX   10  10 ASN A  172  ASN A  181  1                                  10    
HELIX   11  11 GLN A  202  HIS A  212  1                                  11    
HELIX   12  12 PRO A  237  LYS A  240  5                                   4    
HELIX   13  13 ASP A  241  TYR A  251  1                                  11    
HELIX   14  14 THR A  254  ARG A  266  1                                  13    
HELIX   15  15 ASN A  276  GLN A  285  1                                  10    
HELIX   16  16 THR A  292  ALA A  301  1                                  10    
HELIX   17  17 LEU A  311  ARG A  315  5                                   5    
HELIX   18  18 GLY B   35  GLY B   48  1                                  14    
HELIX   19  19 ALA B   55  GLN B   59  5                                   5    
HELIX   20  20 ASN B   60  GLU B   74  1                                  15    
HELIX   21  21 ARG B   78  ILE B   82  5                                   5    
HELIX   22  22 TRP B   89  HIS B   93  5                                   5    
HELIX   23  23 VAL B   94  GLU B   96  5                                   3    
HELIX   24  24 MET B   97  GLN B  110  1                                  14    
HELIX   25  25 ASN B  146  ALA B  160  1                                  15    
HELIX   26  26 ASN B  172  ASN B  181  1                                  10    
HELIX   27  27 GLN B  202  HIS B  212  1                                  11    
HELIX   28  28 PRO B  237  LYS B  240  5                                   4    
HELIX   29  29 ASP B  241  ASN B  252  1                                  12    
HELIX   30  30 THR B  254  ARG B  266  1                                  13    
HELIX   31  31 ASN B  276  GLN B  285  1                                  10    
HELIX   32  32 THR B  292  ALA B  301  1                                  10    
HELIX   33  33 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  LYS A 164   N  VAL A 114           
SHEET    6   B 8 SER A 191  GLU A 195  1  O  GLN A 193   N  VAL A 168           
SHEET    7   B 8 VAL A 215  TYR A 219  1  O  VAL A 215   N  ASN A 192           
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  ILE B 118   N  LEU B  88           
SHEET    5   D 8 VAL B 163  SER B 169  1  O  SER B 165   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           
SHEET    1   E 2 ALA B 124  PHE B 125  0                                        
SHEET    2   E 2 TYR B 142  HIS B 143 -1  O  HIS B 143   N  ALA B 124           
SITE     1 AC1 26 GLY A  24  THR A  25  TYR A  26  ASP A  53                    
SITE     2 AC1 26 TYR A  58  LYS A  87  SER A 169  ASN A 170                    
SITE     3 AC1 26 GLN A 193  TYR A 219  SER A 220  PRO A 221                    
SITE     4 AC1 26 LEU A 222  GLY A 223  THR A 224  SER A 225                    
SITE     5 AC1 26 LEU A 239  ALA A 256  ILE A 271  PRO A 272                    
SITE     6 AC1 26 LYS A 273  SER A 274  PHE A 275  ARG A 279                    
SITE     7 AC1 26 GLU A 282  ASN A 283                                          
SITE     1 AC2 26 GLY B  24  THR B  25  TYR B  26  ASP B  53                    
SITE     2 AC2 26 TYR B  58  LYS B  87  SER B 169  ASN B 170                    
SITE     3 AC2 26 GLN B 193  TYR B 219  SER B 220  PRO B 221                    
SITE     4 AC2 26 LEU B 222  GLY B 223  THR B 224  SER B 225                    
SITE     5 AC2 26 LEU B 239  ALA B 256  ILE B 271  PRO B 272                    
SITE     6 AC2 26 LYS B 273  SER B 274  PHE B 275  ARG B 279                    
SITE     7 AC2 26 GLU B 282  ASN B 283                                          
SITE     1 AC3  4 ASP A 129  GLU B 103  ARG B 107  ASP B 112                    
SITE     1 AC4  2 THR A 224  ARG A 226                                          
SITE     1 AC5  5 TYR A  26  THR A 224  SER A 225  ARG A 226                    
SITE     2 AC5  5 ASN A 227                                                     
CRYST1   49.826  109.833  129.186  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      0.020070 -0.000001 -0.000001        0.00000                         
SCALE2      0.000000  0.009105  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007741        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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