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Database: PDB
Entry: 3LFL
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Original site: 3LFL 
HEADER    TRANSFERASE                             18-JAN-10   3LFL              
TITLE     CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE TRANSFERASE OMEGA 1, DELTA 155 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE OMEGA-1;                         
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: GSTO 1-1;                                                   
COMPND   5 EC: 2.5.1.18;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GSTO1, GSTTLP28;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GLUTATHIONE S-TRANSFERASE OMEGA 1 DEL155, PROTEIN-GLUTATHIONE         
KEYWDS   2 COMPLEX, N-TERMINAL THIOREDOXIN-LIKE DOMAIN, C-TERMINAL ALPHA-       
KEYWDS   3 HELICAL DOMAIN, TRANSFERASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    BROCK J.                                                              
REVDAT   5   09-MAY-12 3LFL    1       REMARK                                   
REVDAT   4   14-DEC-11 3LFL    1       HETATM HETNAM VERSN                      
REVDAT   3   23-FEB-11 3LFL    1       JRNL                                     
REVDAT   2   01-DEC-10 3LFL    1       JRNL                                     
REVDAT   1   24-NOV-10 3LFL    0                                                
JRNL        AUTH   H.ZHOU,J.BROCK,M.G.CASAROTTO,A.J.OAKLEY,P.G.BOARD            
JRNL        TITL   NOVEL FOLDING AND STABILITY DEFECTS CAUSE A DEFICIENCY OF    
JRNL        TITL 2 HUMAN GLUTATHIONE TRANSFERASE OMEGA 1.                       
JRNL        REF    J.BIOL.CHEM.                  V. 286  4271 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21106529                                                     
JRNL        DOI    10.1074/JBC.M110.197822                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 72.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 33943                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1731                            
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 36.5100 -  4.8050    0.83     3289   182  0.1650 0.1940        
REMARK   3     2  4.8050 -  3.8150    0.55     2054   135  0.1540 0.1960        
REMARK   3     3  3.8150 -  3.3330    0.50     1875   106  0.1820 0.2240        
REMARK   3     4  3.3330 -  3.0280    0.54     2052    92  0.2010 0.2510        
REMARK   3     5  3.0280 -  2.8110    0.59     2198   111  0.2090 0.2870        
REMARK   3     6  2.8110 -  2.6460    0.66     2435   141  0.2160 0.2880        
REMARK   3     7  2.6460 -  2.5130    0.74     2719   145  0.2150 0.2900        
REMARK   3     8  2.5130 -  2.4040    0.78     2861   167  0.2250 0.3290        
REMARK   3     9  2.4040 -  2.3110    0.82     3014   155  0.2200 0.2770        
REMARK   3    10  2.3110 -  2.2320    0.86     3150   157  0.2220 0.2920        
REMARK   3    11  2.2320 -  2.1620    0.88     3228   175  0.2280 0.3150        
REMARK   3    12  2.1620 -  2.1000    0.90     3337   165  0.2360 0.2980        
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              : 0.34                                          
REMARK   3   B_SOL              : 37.94                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.820           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.08800                                              
REMARK   3    B22 (A**2) : 0.00700                                              
REMARK   3    B33 (A**2) : -2.09500                                             
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           5768                                  
REMARK   3   ANGLE     :  1.026           7777                                  
REMARK   3   CHIRALITY :  0.070            823                                  
REMARK   3   PLANARITY :  0.011            982                                  
REMARK   3   DIHEDRAL  : 17.617           2213                                  
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 3LFL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057216.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54060                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44498                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 8.800                              
REMARK 200  R MERGE                    (I) : 0.12800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.5, 0.2M TRIMETHYL AMINE   
REMARK 280  N-OXIDE DIHYDRATE, 20% (W/V) POLYETHYLENE GLYCOL MONOMETHYL ETHER   
REMARK 280  2000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.50450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      100.97100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.50450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      100.97100            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
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   BIOMT1   2 -1.000000  0.000000  0.000000       73.00900            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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     SER A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ASN B   231                                                      
REMARK 465     SER B   232                                                      
REMARK 465     PRO B   233                                                      
REMARK 465     GLU B   234                                                      
REMARK 465     ALA B   235                                                      
REMARK 465     CYS B   236                                                      
REMARK 465     ASP B   237                                                      
REMARK 465     TYR B   238                                                      
REMARK 465     GLY B   239                                                      
REMARK 465     LEU B   240                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     GLU C     4                                                      
REMARK 465     LEU C   229                                                      
REMARK 465     GLN C   230                                                      
REMARK 465     ASN C   231                                                      
REMARK 465     SER C   232                                                      
REMARK 465     PRO C   233                                                      
REMARK 465     GLU C   234                                                      
REMARK 465     ALA C   235                                                      
REMARK 465     CYS C   236                                                      
REMARK 465     ASP C   237                                                      
REMARK 465     TYR C   238                                                      
REMARK 465     GLY C   239                                                      
REMARK 465     LEU C   240                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     SER A    5   N    CB   OG                                        
REMARK 480     LYS A  136   CB   CG   CD   CE   NZ                              
REMARK 480     ASP A  138   N                                                   
REMARK 480     SER B    5   N    CA   CB   OG                                   
REMARK 480     GLN B  134   CG   CD   OE1  NE2                                  
REMARK 480     LYS B  136   CG   CD   CE   NZ                                   
REMARK 480     GLU B  137   CB   CG   CD   OE1  OE2                             
REMARK 480     LYS C  136   CD   CE   NZ                                        
REMARK 480     TYR C  139   CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 480     LYS C  143   CD   CE   NZ                                        
REMARK 480     SER C  217   CB   OG                                             
REMARK 480     LYS C  219   CG   CD   CE   NZ                                   
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    ASN A  58       66.04   -116.46                                   
REMARK 500    GLU A  85      112.16     73.51                                   
REMARK 500    ASN A 158       60.15     39.02                                   
REMARK 500    ALA B   6       17.02    176.12                                   
REMARK 500    GLU B  85      111.89     73.97                                   
REMARK 500    ASP B 138      -70.26    -60.25                                   
REMARK 500    ASN B 158      -75.23    -24.42                                   
REMARK 500    LYS B 187       35.21     71.30                                   
REMARK 500    ALA C   6      114.94    169.77                                   
REMARK 500    ARG C   7      149.09    108.01                                   
REMARK 500    ASN C  58       74.17   -163.12                                   
REMARK 500    GLU C  85      115.12     74.18                                   
REMARK 500    SER C 133      102.89     -5.26                                   
REMARK 500    GLU C 226      -66.56     64.40                                   
REMARK 500    LEU C 227       47.36    -76.89                                   
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 GSH A 241                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 242                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 241                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT B 242                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT C 241                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH C 242                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EEM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE TRANSFERASE OMEGA 1           
REMARK 900 NATIVE                                                               
DBREF  3LFL A    1   240  UNP    P78417   GSTO1_HUMAN      1    241             
DBREF  3LFL B    1   240  UNP    P78417   GSTO1_HUMAN      1    241             
DBREF  3LFL C    1   240  UNP    P78417   GSTO1_HUMAN      1    241             
SEQADV 3LFL     A       UNP  P78417    GLU   154 DELETION                       
SEQADV 3LFL     B       UNP  P78417    GLU   154 DELETION                       
SEQADV 3LFL     C       UNP  P78417    GLU   154 DELETION                       
SEQRES   1 A  240  MET SER GLY GLU SER ALA ARG SER LEU GLY LYS GLY SER          
SEQRES   2 A  240  ALA PRO PRO GLY PRO VAL PRO GLU GLY SER ILE ARG ILE          
SEQRES   3 A  240  TYR SER MET ARG PHE CYS PRO PHE ALA GLU ARG THR ARG          
SEQRES   4 A  240  LEU VAL LEU LYS ALA LYS GLY ILE ARG HIS GLU VAL ILE          
SEQRES   5 A  240  ASN ILE ASN LEU LYS ASN LYS PRO GLU TRP PHE PHE LYS          
SEQRES   6 A  240  LYS ASN PRO PHE GLY LEU VAL PRO VAL LEU GLU ASN SER          
SEQRES   7 A  240  GLN GLY GLN LEU ILE TYR GLU SER ALA ILE THR CYS GLU          
SEQRES   8 A  240  TYR LEU ASP GLU ALA TYR PRO GLY LYS LYS LEU LEU PRO          
SEQRES   9 A  240  ASP ASP PRO TYR GLU LYS ALA CYS GLN LYS MET ILE LEU          
SEQRES  10 A  240  GLU LEU PHE SER LYS VAL PRO SER LEU VAL GLY SER PHE          
SEQRES  11 A  240  ILE ARG SER GLN ASN LYS GLU ASP TYR ALA GLY LEU LYS          
SEQRES  12 A  240  GLU GLU PHE ARG LYS GLU PHE THR LYS LEU GLU VAL LEU          
SEQRES  13 A  240  THR ASN LYS LYS THR THR PHE PHE GLY GLY ASN SER ILE          
SEQRES  14 A  240  SER MET ILE ASP TYR LEU ILE TRP PRO TRP PHE GLU ARG          
SEQRES  15 A  240  LEU GLU ALA MET LYS LEU ASN GLU CYS VAL ASP HIS THR          
SEQRES  16 A  240  PRO LYS LEU LYS LEU TRP MET ALA ALA MET LYS GLU ASP          
SEQRES  17 A  240  PRO THR VAL SER ALA LEU LEU THR SER GLU LYS ASP TRP          
SEQRES  18 A  240  GLN GLY PHE LEU GLU LEU TYR LEU GLN ASN SER PRO GLU          
SEQRES  19 A  240  ALA CYS ASP TYR GLY LEU                                      
SEQRES   1 B  240  MET SER GLY GLU SER ALA ARG SER LEU GLY LYS GLY SER          
SEQRES   2 B  240  ALA PRO PRO GLY PRO VAL PRO GLU GLY SER ILE ARG ILE          
SEQRES   3 B  240  TYR SER MET ARG PHE CYS PRO PHE ALA GLU ARG THR ARG          
SEQRES   4 B  240  LEU VAL LEU LYS ALA LYS GLY ILE ARG HIS GLU VAL ILE          
SEQRES   5 B  240  ASN ILE ASN LEU LYS ASN LYS PRO GLU TRP PHE PHE LYS          
SEQRES   6 B  240  LYS ASN PRO PHE GLY LEU VAL PRO VAL LEU GLU ASN SER          
SEQRES   7 B  240  GLN GLY GLN LEU ILE TYR GLU SER ALA ILE THR CYS GLU          
SEQRES   8 B  240  TYR LEU ASP GLU ALA TYR PRO GLY LYS LYS LEU LEU PRO          
SEQRES   9 B  240  ASP ASP PRO TYR GLU LYS ALA CYS GLN LYS MET ILE LEU          
SEQRES  10 B  240  GLU LEU PHE SER LYS VAL PRO SER LEU VAL GLY SER PHE          
SEQRES  11 B  240  ILE ARG SER GLN ASN LYS GLU ASP TYR ALA GLY LEU LYS          
SEQRES  12 B  240  GLU GLU PHE ARG LYS GLU PHE THR LYS LEU GLU VAL LEU          
SEQRES  13 B  240  THR ASN LYS LYS THR THR PHE PHE GLY GLY ASN SER ILE          
SEQRES  14 B  240  SER MET ILE ASP TYR LEU ILE TRP PRO TRP PHE GLU ARG          
SEQRES  15 B  240  LEU GLU ALA MET LYS LEU ASN GLU CYS VAL ASP HIS THR          
SEQRES  16 B  240  PRO LYS LEU LYS LEU TRP MET ALA ALA MET LYS GLU ASP          
SEQRES  17 B  240  PRO THR VAL SER ALA LEU LEU THR SER GLU LYS ASP TRP          
SEQRES  18 B  240  GLN GLY PHE LEU GLU LEU TYR LEU GLN ASN SER PRO GLU          
SEQRES  19 B  240  ALA CYS ASP TYR GLY LEU                                      
SEQRES   1 C  240  MET SER GLY GLU SER ALA ARG SER LEU GLY LYS GLY SER          
SEQRES   2 C  240  ALA PRO PRO GLY PRO VAL PRO GLU GLY SER ILE ARG ILE          
SEQRES   3 C  240  TYR SER MET ARG PHE CYS PRO PHE ALA GLU ARG THR ARG          
SEQRES   4 C  240  LEU VAL LEU LYS ALA LYS GLY ILE ARG HIS GLU VAL ILE          
SEQRES   5 C  240  ASN ILE ASN LEU LYS ASN LYS PRO GLU TRP PHE PHE LYS          
SEQRES   6 C  240  LYS ASN PRO PHE GLY LEU VAL PRO VAL LEU GLU ASN SER          
SEQRES   7 C  240  GLN GLY GLN LEU ILE TYR GLU SER ALA ILE THR CYS GLU          
SEQRES   8 C  240  TYR LEU ASP GLU ALA TYR PRO GLY LYS LYS LEU LEU PRO          
SEQRES   9 C  240  ASP ASP PRO TYR GLU LYS ALA CYS GLN LYS MET ILE LEU          
SEQRES  10 C  240  GLU LEU PHE SER LYS VAL PRO SER LEU VAL GLY SER PHE          
SEQRES  11 C  240  ILE ARG SER GLN ASN LYS GLU ASP TYR ALA GLY LEU LYS          
SEQRES  12 C  240  GLU GLU PHE ARG LYS GLU PHE THR LYS LEU GLU VAL LEU          
SEQRES  13 C  240  THR ASN LYS LYS THR THR PHE PHE GLY GLY ASN SER ILE          
SEQRES  14 C  240  SER MET ILE ASP TYR LEU ILE TRP PRO TRP PHE GLU ARG          
SEQRES  15 C  240  LEU GLU ALA MET LYS LEU ASN GLU CYS VAL ASP HIS THR          
SEQRES  16 C  240  PRO LYS LEU LYS LEU TRP MET ALA ALA MET LYS GLU ASP          
SEQRES  17 C  240  PRO THR VAL SER ALA LEU LEU THR SER GLU LYS ASP TRP          
SEQRES  18 C  240  GLN GLY PHE LEU GLU LEU TYR LEU GLN ASN SER PRO GLU          
SEQRES  19 C  240  ALA CYS ASP TYR GLY LEU                                      
HET    GSH  A 241      20                                                       
HET    DTT  A 242       8                                                       
HET    GSH  B 241      20                                                       
HET    DTT  B 242       8                                                       
HET    DTT  C 241       8                                                       
HET    GSH  C 242      20                                                       
HETNAM     GSH GLUTATHIONE                                                      
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
FORMUL   4  GSH    3(C10 H17 N3 O6 S)                                           
FORMUL   5  DTT    3(C4 H10 O2 S2)                                              
FORMUL  10  HOH   *328(H2 O)                                                    
HELIX    1   1 CYS A   32  LYS A   45  1                                  14    
HELIX    2   2 PRO A   60  LYS A   66  5                                   7    
HELIX    3   3 GLU A   85  TYR A   97  1                                  13    
HELIX    4   4 ASP A  106  PHE A  120  1                                  15    
HELIX    5   5 LYS A  122  ARG A  132  1                                  11    
HELIX    6   6 ASN A  135  THR A  157  1                                  23    
HELIX    7   7 SER A  170  MET A  186  1                                  17    
HELIX    8   8 LEU A  188  ASP A  193  5                                   6    
HELIX    9   9 THR A  195  ASP A  208  1                                  14    
HELIX   10  10 ASP A  208  LEU A  215  1                                   8    
HELIX   11  11 SER A  217  GLN A  230  1                                  14    
HELIX   12  12 SER A  232  TYR A  238  5                                   7    
HELIX   13  13 CYS B   32  LYS B   45  1                                  14    
HELIX   14  14 TRP B   62  ASN B   67  1                                   6    
HELIX   15  15 GLU B   85  TYR B   97  1                                  13    
HELIX   16  16 ASP B  106  PHE B  120  1                                  15    
HELIX   17  17 LYS B  122  ARG B  132  1                                  11    
HELIX   18  18 ASN B  135  LEU B  156  1                                  22    
HELIX   19  19 SER B  170  ARG B  182  1                                  13    
HELIX   20  20 ARG B  182  LYS B  187  1                                   6    
HELIX   21  21 LEU B  188  ASP B  193  5                                   6    
HELIX   22  22 THR B  195  ASP B  208  1                                  14    
HELIX   23  23 ASP B  208  LEU B  214  1                                   7    
HELIX   24  24 SER B  217  ASP B  220  5                                   4    
HELIX   25  25 TRP B  221  GLN B  230  1                                  10    
HELIX   26  26 CYS C   32  LYS C   45  1                                  14    
HELIX   27  27 TRP C   62  ASN C   67  1                                   6    
HELIX   28  28 GLU C   85  TYR C   97  1                                  13    
HELIX   29  29 ASP C  106  SER C  121  1                                  16    
HELIX   30  30 LYS C  122  SER C  133  1                                  12    
HELIX   31  31 GLU C  137  ASN C  158  1                                  22    
HELIX   32  32 SER C  170  ARG C  182  1                                  13    
HELIX   33  33 LEU C  188  ASP C  193  5                                   6    
HELIX   34  34 THR C  195  ASP C  208  1                                  14    
HELIX   35  35 ASP C  208  LEU C  215  1                                   8    
HELIX   36  36 SER C  217  PHE C  224  5                                   8    
SHEET    1   A 4 HIS A  49  ASN A  53  0                                        
SHEET    2   A 4 ILE A  24  SER A  28  1  N  ILE A  26   O  GLU A  50           
SHEET    3   A 4 VAL A  74  ASN A  77 -1  O  VAL A  74   N  TYR A  27           
SHEET    4   A 4 LEU A  82  TYR A  84 -1  O  ILE A  83   N  LEU A  75           
SHEET    1   B 4 HIS B  49  ASN B  53  0                                        
SHEET    2   B 4 ILE B  24  SER B  28  1  N  ILE B  26   O  GLU B  50           
SHEET    3   B 4 VAL B  74  ASN B  77 -1  O  VAL B  74   N  TYR B  27           
SHEET    4   B 4 LEU B  82  TYR B  84 -1  O  ILE B  83   N  LEU B  75           
SHEET    1   C 4 HIS C  49  ASN C  53  0                                        
SHEET    2   C 4 ILE C  24  SER C  28  1  N  ILE C  26   O  ILE C  52           
SHEET    3   C 4 VAL C  74  ASN C  77 -1  O  GLU C  76   N  ARG C  25           
SHEET    4   C 4 LEU C  82  TYR C  84 -1  O  ILE C  83   N  LEU C  75           
CISPEP   1 VAL A   72    PRO A   73          0         1.56                     
CISPEP   2 VAL B   72    PRO B   73          0        -0.70                     
CISPEP   3 ASN B  158    LYS B  159          0        -9.05                     
CISPEP   4 VAL C   72    PRO C   73          0         8.38                     
SITE     1 AC1 13 CYS A  32  PHE A  34  LEU A  56  LYS A  59                    
SITE     2 AC1 13 LEU A  71  VAL A  72  PRO A  73  GLU A  85                    
SITE     3 AC1 13 SER A  86  HOH A 248  HOH A 275  HOH A 304                    
SITE     4 AC1 13 HOH A 362                                                     
SITE     1 AC2  3 LYS A 143  ARG A 147  CYS A 191                               
SITE     1 AC3 10 CYS B  32  PHE B  34  LYS B  59  LEU B  71                    
SITE     2 AC3 10 VAL B  72  PRO B  73  GLU B  85  SER B  86                    
SITE     3 AC3 10 HOH B 271  HOH B 294                                          
SITE     1 AC4  5 LYS B 143  ARG B 147  GLU B 190  CYS B 191                    
SITE     2 AC4  5 HOH B 283                                                     
SITE     1 AC5  2 ARG C 147  CYS C 191                                          
SITE     1 AC6 12 CYS C  32  PHE C  34  LEU C  56  LYS C  59                    
SITE     2 AC6 12 LEU C  71  VAL C  72  PRO C  73  GLU C  85                    
SITE     3 AC6 12 SER C  86  HOH C 244  HOH C 289  HOH C 298                    
CRYST1   73.009  201.942   53.387  90.00  90.00  90.00 P 21 21 2    12          
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      0.013697  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004952  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018731        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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