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PDBsum entry 6gss

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
6gss
Jmol
Contents
Protein chain
208 a.a. *
Ligands
GSH ×2
MES ×2
Waters ×138
* Residue conservation analysis
HEADER    TRANSFERASE                             13-AUG-97   6GSS
TITLE     HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE P1-1;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: TWO INTACT MONOMERS;
COMPND   5 SYNONYM: GSTP1-1;
COMPND   6 EC: 2.5.1.18;
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: PLACENTA;
SOURCE   6 CELLULAR_LOCATION: CYTOPLASM;
SOURCE   7 GENE: GTP_HUMAN;
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    TRANSFERASE, GLUTATHIONE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.OAKLEY,M.PARKER
REVDAT   4   21-DEC-11 6GSS    1       FORMUL HET    VERSN
REVDAT   3   24-FEB-09 6GSS    1       VERSN
REVDAT   2   01-APR-03 6GSS    1       JRNL
REVDAT   1   16-SEP-98 6GSS    0
JRNL        AUTH   A.J.OAKLEY,M.L.BELLO,A.BATTISTONI,G.RICCI,J.ROSSJOHN,
JRNL        AUTH 2 H.O.VILLAR,M.W.PARKER
JRNL        TITL   THE STRUCTURES OF HUMAN GLUTATHIONE TRANSFERASE P1-1 IN
JRNL        TITL 2 COMPLEX WITH GLUTATHIONE AND VARIOUS INHIBITORS AT HIGH
JRNL        TITL 3 RESOLUTION.
JRNL        REF    J.MOL.BIOL.                   V. 274    84 1997
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   9398518
JRNL        DOI    10.1006/JMBI.1997.1364
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   P.REINEMER,H.W.DIRR,R.LADENSTEIN,R.HUBER,M.LO BELLO,
REMARK   1  AUTH 2 G.FEDERICI,M.W.PARKER
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE
REMARK   1  TITL 2 S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH
REMARK   1  TITL 3 S-HEXYLGLUTATHIONE AT 2.8 A RESOLUTION
REMARK   1  REF    J.MOL.BIOL.                   V. 227   214 1992
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.6
REMARK   3   NUMBER OF REFLECTIONS             : 31318
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.200
REMARK   3   FREE R VALUE                     : 0.218
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.300
REMARK   3   FREE R VALUE TEST SET COUNT      : 1635
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.000
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.99
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 68.85
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3086
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2990
REMARK   3   BIN FREE R VALUE                    : 0.2970
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.51
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 166
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3262
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 64
REMARK   3   SOLVENT ATOMS            : 138
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.012
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.20
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.20
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : RESTRAINTS
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 6GSS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-96
REMARK 200  TEMPERATURE           (KELVIN) : 288
REMARK 200  PH                             : 5.4
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 RUH2R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32970
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.0
REMARK 200  DATA REDUNDANCY                : 3.300
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08500
REMARK 200   FOR THE DATA SET  : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94
REMARK 200  COMPLETENESS FOR SHELL     (%) : 66.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.26200
REMARK 200   FOR SHELL         : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 1GSS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.4
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       39.61000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.34500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       39.61000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       45.34500
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: 3920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 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     PRO A     1
REMARK 465     PRO B     1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A  64      111.82     80.11
REMARK 500    ASN A 110       67.84   -155.03
REMARK 500    THR A 141     -111.72   -111.36
REMARK 500    GLN B  64      111.76     80.18
REMARK 500    ASN B 110       67.75   -154.71
REMARK 500    THR B 141     -111.59   -111.60
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 269        DISTANCE =  5.98 ANGSTROMS
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 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 211
DBREF  6GSS A    1   209  UNP    P09211   GSTP1_HUMAN      1    209
DBREF  6GSS B    1   209  UNP    P09211   GSTP1_HUMAN      1    209
SEQRES   1 A  209  PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG
SEQRES   2 A  209  CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN
SEQRES   3 A  209  SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN
SEQRES   4 A  209  GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU
SEQRES   5 A  209  PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER
SEQRES   6 A  209  ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU
SEQRES   7 A  209  TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET
SEQRES   8 A  209  VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE
SEQRES   9 A  209  SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP
SEQRES  10 A  209  TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU
SEQRES  11 A  209  THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE
SEQRES  12 A  209  VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU
SEQRES  13 A  209  ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS
SEQRES  14 A  209  LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG
SEQRES  15 A  209  LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER
SEQRES  16 A  209  PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS
SEQRES  17 A  209  GLN
SEQRES   1 B  209  PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG
SEQRES   2 B  209  CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN
SEQRES   3 B  209  SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN
SEQRES   4 B  209  GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU
SEQRES   5 B  209  PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER
SEQRES   6 B  209  ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU
SEQRES   7 B  209  TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET
SEQRES   8 B  209  VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE
SEQRES   9 B  209  SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP
SEQRES  10 B  209  TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU
SEQRES  11 B  209  THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE
SEQRES  12 B  209  VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU
SEQRES  13 B  209  ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS
SEQRES  14 B  209  LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG
SEQRES  15 B  209  LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER
SEQRES  16 B  209  PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS
SEQRES  17 B  209  GLN
HET    GSH  A 210      20
HET    MES  A 211      12
HET    GSH  B 210      20
HET    MES  B 211      12
HETNAM     GSH GLUTATHIONE
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL   3  GSH    2(C10 H17 N3 O6 S)
FORMUL   4  MES    2(C6 H13 N O4 S)
FORMUL   7  HOH   *138(H2 O)
HELIX    1   1 GLY A   12  ASP A   23  5                                  12
HELIX    2   2 VAL A   35  GLU A   40  1                                   6
HELIX    3   3 SER A   42  SER A   46  1                                   5
HELIX    4   4 SER A   65  LEU A   76  1                                  12
HELIX    5   5 GLN A   83  THR A  109  1                                  27
HELIX    6   6 TYR A  111  SER A  134  1                                  24
HELIX    7   7 GLN A  137  GLY A  139  5                                   3
HELIX    8   8 PHE A  150  LEU A  165  1                                  16
HELIX    9   9 PRO A  174  SER A  184  1                                  11
HELIX   10  10 PRO A  187  ALA A  194  1                                   8
HELIX   11  11 PRO A  196  VAL A  199  1                                   4
HELIX   12  12 GLY B   12  ASP B   23  5                                  12
HELIX   13  13 VAL B   35  GLU B   40  1                                   6
HELIX   14  14 SER B   42  SER B   46  1                                   5
HELIX   15  15 SER B   65  LEU B   76  1                                  12
HELIX   16  16 GLN B   83  THR B  109  1                                  27
HELIX   17  17 TYR B  111  SER B  134  1                                  24
HELIX   18  18 GLN B  137  GLY B  139  5                                   3
HELIX   19  19 PHE B  150  LEU B  165  1                                  16
HELIX   20  20 PRO B  174  ALA B  185  1                                  12
HELIX   21  21 PRO B  187  ALA B  194  1                                   8
HELIX   22  22 PRO B  196  VAL B  199  1                                   4
SHEET    1   A 4 TRP A  28  VAL A  33  0
SHEET    2   A 4 TYR A   3  PHE A   8  1  N  TYR A   3   O  LYS A  29
SHEET    3   A 4 LYS A  54  ASP A  57 -1  N  GLN A  56   O  THR A   4
SHEET    4   A 4 LEU A  60  TYR A  63 -1  N  LEU A  62   O  PHE A  55
SHEET    1   B 4 TRP B  28  VAL B  33  0
SHEET    2   B 4 TYR B   3  PHE B   8  1  N  TYR B   3   O  LYS B  29
SHEET    3   B 4 LYS B  54  ASP B  57 -1  N  GLN B  56   O  THR B   4
SHEET    4   B 4 LEU B  60  TYR B  63 -1  N  LEU B  62   O  PHE B  55
CISPEP   1 LEU A   52    PRO A   53          0         1.50
CISPEP   2 LEU B   52    PRO B   53          0         1.28
SITE     1 AC1 11 TYR A   7  PHE A   8  ARG A  13  TRP A  38
SITE     2 AC1 11 LYS A  44  GLY A  50  GLN A  51  LEU A  52
SITE     3 AC1 11 GLN A  64  SER A  65  ASP B  98
SITE     1 AC2  5 TRP A  28  GLU A  30  GLU A 197  HOH A 268
SITE     2 AC2  5 ASP B 171
SITE     1 AC3 11 ASP A  98  TYR B   7  PHE B   8  ARG B  13
SITE     2 AC3 11 TRP B  38  LYS B  44  GLY B  50  GLN B  51
SITE     3 AC3 11 LEU B  52  GLN B  64  SER B  65
SITE     1 AC4  5 ASP A 171  HOH A 241  TRP B  28  GLU B  30
SITE     2 AC4  5 GLU B 197
CRYST1   79.220   90.690   69.170  90.00  98.22  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      0.012623  0.000000  0.001824        0.00000
SCALE2      0.000000  0.011027  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014607        0.00000
MTRIX1   1  0.945273  0.096347  0.311730       -5.44120    1
MTRIX2   1  0.096767 -0.995206  0.014157       22.08816    1
MTRIX3   1  0.311600  0.016783 -0.950065       27.61167    1
      
PROCHECK
Go to PROCHECK summary
 References