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PDBsum entry 1mtc

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
1mtc
Jmol
Contents
Protein chains
217 a.a. *
Ligands
GPR ×2
Waters ×185
* Residue conservation analysis
HEADER    TRANSFERASE                             20-SEP-02   1MTC
TITLE     GLUTATHIONE TRANSFERASE MUTANT Y115F
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE YB1;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CHAIN 3; GST M1-1; GST CLASS-MU 1; GLUTATHIONE S-
COMPND   5 TRANSFERASE YB-1 SUBUNIT;
COMPND   6 EC: 2.5.1.18;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES;
COMPND   9 OTHER_DETAILS: COMPLEX WITH (9R,10R)-9-(S-GLUTATHIONYL)-10-
COMPND  10 HYDROXY-9,10-DIHROPHENANTHRENE
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;
SOURCE   4 ORGANISM_TAXID: 10116;
SOURCE   5 ORGAN: LIVER;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGT33MX
KEYWDS    GLUTATHIONE TRANSFERASE, PROTEIN DYNAMICS, PROTEIN CATALYSIS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.E.LADNER,G.XIAO,R.N.ARMSTRONG,G.L.GILLILAND
REVDAT   2   24-FEB-09 1MTC    1       VERSN
REVDAT   1   25-MAR-03 1MTC    0
JRNL        AUTH   S.G.CODREANU,J.E.LADNER,G.XIAO,N.V.STOURMAN,
JRNL        AUTH 2 D.L.HACHEY,G.L.GILLILAND,R.N.ARMSTRONG
JRNL        TITL   LOCAL PROTEIN DYNAMICS AND CATALYSIS: DETECTION OF
JRNL        TITL 2 SEGMENTAL MOTION ASSOCIATED WITH RATE-LIMITING
JRNL        TITL 3 PRODUCT RELEASE BY A GLUTATHIONE TRANSFERASE
JRNL        REF    BIOCHEMISTRY                  V.  41 15161 2002
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   12484753
JRNL        DOI    10.1021/BI026776P
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.20 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) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6
REMARK   3   CROSS-VALIDATION METHOD           : FREE R
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) : 0.203
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 21775
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.187
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)) : 18747
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 3632
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 70
REMARK   3   SOLVENT ATOMS      : 185
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3889.00
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 15571
REMARK   3   NUMBER OF RESTRAINTS                     : 15303
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.011
REMARK   3   ANGLE DISTANCES                      (A) : 0.039
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.015
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.016
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.022
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.015
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.044
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 : ENGH & HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK   3  METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
REMARK   4
REMARK   4 1MTC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-02.
REMARK 100 THE RCSB ID CODE IS RCSB017169.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-95
REMARK 200  TEMPERATURE           (KELVIN) : 143
REMARK 200  PH                             : 8.0
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          : SIEMENS
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : BRUKER
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200  DATA SCALING SOFTWARE          : XENGEN
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21775
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0
REMARK 200  DATA REDUNDANCY                : 3.000
REMARK 200  R MERGE                    (I) : 0.11000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 33.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.23000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 8.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: 3GST
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONOIUM SULFATE AT PH 8.0, VAPOR
REMARK 280  DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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       43.37500
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.29000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       43.37500
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.29000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 4650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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    ARG A  10   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    TYR A  22   CB  -  CG  -  CD2 ANGL. DEV. =  -5.3 DEGREES
REMARK 500    SER A  26   N   -  CA  -  CB  ANGL. DEV. =  11.3 DEGREES
REMARK 500    ARG A  31   CD  -  NE  -  CZ  ANGL. DEV. =   9.0 DEGREES
REMARK 500    ARG A  31   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG A  42   CD  -  NE  -  CZ  ANGL. DEV. =   9.3 DEGREES
REMARK 500    ARG A  42   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    TYR A  61   CB  -  CG  -  CD1 ANGL. DEV. =   8.2 DEGREES
REMARK 500    TYR A  61   CG  -  CD1 -  CE1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP A  64   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG A  67   CD  -  NE  -  CZ  ANGL. DEV. =  16.6 DEGREES
REMARK 500    ARG A  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG A  77   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    TYR A  78   CB  -  CG  -  CD1 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    ARG A  81   CD  -  NE  -  CZ  ANGL. DEV. = -12.4 DEGREES
REMARK 500    HIS A  84   CA  -  CB  -  CG  ANGL. DEV. = -10.9 DEGREES
REMARK 500    ARG A 107   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    ARG A 144   CD  -  NE  -  CZ  ANGL. DEV. =  10.8 DEGREES
REMARK 500    ARG A 144   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ARG A 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    TYR A 154   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    TYR A 154   CB  -  CG  -  CD1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    TYR A 160   CB  -  CG  -  CD1 ANGL. DEV. =   5.2 DEGREES
REMARK 500    TYR A 196   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    TYR A 196   CB  -  CG  -  CD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG B  10   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ARG B  10   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG B  42   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG B  42   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES
REMARK 500    TYR B  61   CB  -  CG  -  CD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG B  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG B  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.9 DEGREES
REMARK 500    GLU B  92   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.5 DEGREES
REMARK 500    ARG B  95   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ASP B  97   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    GLU B 100   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.3 DEGREES
REMARK 500    PHE B 115   CB  -  CG  -  CD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG B 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    ARG B 186   CD  -  NE  -  CZ  ANGL. DEV. =  15.6 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    GLN A  71      111.01     80.81
REMARK 500    HIS A  84       55.34     39.88
REMARK 500    ASP A 118       29.36    -79.72
REMARK 500    LEU A 203       87.95   -153.72
REMARK 500    LYS A 210        1.21    -68.23
REMARK 500    ASN B   8       54.13    -96.00
REMARK 500    TYR B  40       43.60     71.57
REMARK 500    PHE B  56       79.35   -118.40
REMARK 500    GLN B  71      110.25     81.50
REMARK 500    PHE B 177       69.82   -119.00
REMARK 500    SER B 209     -138.73    -59.75
REMARK 500    LEU B 211       20.44    -59.41
REMARK 500    GLN B 213       33.91    -96.66
REMARK 500    TRP B 214      139.75   -174.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 443        DISTANCE =  5.88 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GPR A 5218
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GPR B 6218
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GST   RELATED DB: PDB
DBREF  1MTC A    1   217  UNP    P04905   GSTM1_RAT        1    217
DBREF  1MTC B    1   217  UNP    P04905   GSTM1_RAT        1    217
SEQADV 1MTC PHE A  115  UNP  P04905    TYR   115 ENGINEERED
SEQADV 1MTC PHE B  115  UNP  P04905    TYR   115 ENGINEERED
SEQRES   1 A  217  PRO MET ILE LEU GLY TYR TRP ASN VAL ARG GLY LEU THR
SEQRES   2 A  217  HIS PRO ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER
SEQRES   3 A  217  TYR GLU GLU LYS ARG TYR ALA MET GLY ASP ALA PRO ASP
SEQRES   4 A  217  TYR ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU
SEQRES   5 A  217  GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY
SEQRES   6 A  217  SER ARG LYS ILE THR GLN SER ASN ALA ILE MET ARG TYR
SEQRES   7 A  217  LEU ALA ARG LYS HIS HIS LEU CYS GLY GLU THR GLU GLU
SEQRES   8 A  217  GLU ARG ILE ARG ALA ASP ILE VAL GLU ASN GLN VAL MET
SEQRES   9 A  217  ASP ASN ARG MET GLN LEU ILE MET LEU CYS PHE ASN PRO
SEQRES  10 A  217  ASP PHE GLU LYS GLN LYS PRO GLU PHE LEU LYS THR ILE
SEQRES  11 A  217  PRO GLU LYS MET LYS LEU TYR SER GLU PHE LEU GLY LYS
SEQRES  12 A  217  ARG PRO TRP PHE ALA GLY ASP LYS VAL THR TYR VAL ASP
SEQRES  13 A  217  PHE LEU ALA TYR ASP ILE LEU ASP GLN TYR HIS ILE PHE
SEQRES  14 A  217  GLU PRO LYS CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP
SEQRES  15 A  217  PHE LEU ALA ARG PHE GLU GLY LEU LYS LYS ILE SER ALA
SEQRES  16 A  217  TYR MET LYS SER SER ARG TYR LEU SER THR PRO ILE PHE
SEQRES  17 A  217  SER LYS LEU ALA GLN TRP SER ASN LYS
SEQRES   1 B  217  PRO MET ILE LEU GLY TYR TRP ASN VAL ARG GLY LEU THR
SEQRES   2 B  217  HIS PRO ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER
SEQRES   3 B  217  TYR GLU GLU LYS ARG TYR ALA MET GLY ASP ALA PRO ASP
SEQRES   4 B  217  TYR ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU
SEQRES   5 B  217  GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY
SEQRES   6 B  217  SER ARG LYS ILE THR GLN SER ASN ALA ILE MET ARG TYR
SEQRES   7 B  217  LEU ALA ARG LYS HIS HIS LEU CYS GLY GLU THR GLU GLU
SEQRES   8 B  217  GLU ARG ILE ARG ALA ASP ILE VAL GLU ASN GLN VAL MET
SEQRES   9 B  217  ASP ASN ARG MET GLN LEU ILE MET LEU CYS PHE ASN PRO
SEQRES  10 B  217  ASP PHE GLU LYS GLN LYS PRO GLU PHE LEU LYS THR ILE
SEQRES  11 B  217  PRO GLU LYS MET LYS LEU TYR SER GLU PHE LEU GLY LYS
SEQRES  12 B  217  ARG PRO TRP PHE ALA GLY ASP LYS VAL THR TYR VAL ASP
SEQRES  13 B  217  PHE LEU ALA TYR ASP ILE LEU ASP GLN TYR HIS ILE PHE
SEQRES  14 B  217  GLU PRO LYS CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP
SEQRES  15 B  217  PHE LEU ALA ARG PHE GLU GLY LEU LYS LYS ILE SER ALA
SEQRES  16 B  217  TYR MET LYS SER SER ARG TYR LEU SER THR PRO ILE PHE
SEQRES  17 B  217  SER LYS LEU ALA GLN TRP SER ASN LYS
HET    GPR  A5218      35
HET    GPR  B6218      35
HETNAM     GPR (9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-
HETNAM   2 GPR  DIHYDROPHENANTHRENE
FORMUL   3  GPR    2(C24 H27 N3 O7 S)
FORMUL   5  HOH   *185(H2 O)
HELIX    1   1 THR A   13  THR A   23  1                                  11
HELIX    2   2 ARG A   42  ASN A   47  1                                   6
HELIX    3   3 GLU A   48  LEU A   52  5                                   5
HELIX    4   4 GLN A   71  HIS A   83  1                                  13
HELIX    5   5 THR A   89  PHE A  115  1                                  27
HELIX    6   6 ASP A  118  GLY A  142  1                                  25
HELIX    7   7 THR A  153  GLU A  170  1                                  18
HELIX    8   8 PRO A  171  ASP A  175  5                                   5
HELIX    9   9 PHE A  177  LEU A  190  1                                  14
HELIX   10  10 LEU A  190  LYS A  198  1                                   9
HELIX   11  11 THR B   13  THR B   23  1                                  11
HELIX   12  12 ARG B   42  PHE B   50  1                                   9
HELIX   13  13 GLN B   71  HIS B   83  1                                  13
HELIX   14  14 THR B   89  PHE B  115  1                                  27
HELIX   15  15 ASP B  118  GLY B  142  1                                  25
HELIX   16  16 THR B  153  GLU B  170  1                                  18
HELIX   17  17 PHE B  177  LEU B  190  1                                  14
HELIX   18  18 LEU B  190  LYS B  198  1                                   9
SHEET    1   A 4 TYR A  27  TYR A  32  0
SHEET    2   A 4 MET A   2  TRP A   7  1  N  MET A   2   O  GLU A  28
SHEET    3   A 4 TYR A  61  ASP A  64 -1  O  TYR A  61   N  GLY A   5
SHEET    4   A 4 ARG A  67  THR A  70 -1  O  ILE A  69   N  LEU A  62
SHEET    1   B 4 TYR B  27  TYR B  32  0
SHEET    2   B 4 MET B   2  TRP B   7  1  N  MET B   2   O  GLU B  28
SHEET    3   B 4 TYR B  61  ASP B  64 -1  O  ILE B  63   N  ILE B   3
SHEET    4   B 4 ARG B  67  THR B  70 -1  O  ARG B  67   N  ASP B  64
CISPEP   1 ALA A   37    PRO A   38          0        -1.34
CISPEP   2 LEU A   59    PRO A   60          0        -0.35
CISPEP   3 THR A  205    PRO A  206          0        -4.86
CISPEP   4 ALA B   37    PRO B   38          0        -1.06
CISPEP   5 LEU B   59    PRO B   60          0         0.01
CISPEP   6 THR B  205    PRO B  206          0        -2.06
SITE     1 AC1 22 TYR A   6  TRP A   7  LEU A  12  ARG A  42
SITE     2 AC1 22 TRP A  45  LYS A  49  ASN A  58  LEU A  59
SITE     3 AC1 22 PRO A  60  GLN A  71  SER A  72  MET A 104
SITE     4 AC1 22 MET A 108  ILE A 111  PHE A 208  SER A 209
SITE     5 AC1 22 HOH A 306  HOH A 313  HOH A 315  HOH A 380
SITE     6 AC1 22 HOH A 415  ASP B 105
SITE     1 AC2 18 ASP A 105  TYR B   6  TRP B   7  GLY B  11
SITE     2 AC2 18 LEU B  12  TRP B  45  LYS B  49  ASN B  58
SITE     3 AC2 18 LEU B  59  GLN B  71  SER B  72  MET B 104
SITE     4 AC2 18 ILE B 111  PHE B 115  SER B 209  HOH B 329
SITE     5 AC2 18 HOH B 333  HOH B 367
CRYST1   86.750   68.580   80.460  90.00 105.12  90.00 C 1 2 1       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      0.011527  0.000000  0.003115        0.00000
SCALE2      0.000000  0.014582  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012874        0.00000
      
PROCHECK
Go to PROCHECK summary
 References