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PDBsum entry 2c80

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
2c80
Jmol
Contents
Protein chains
208 a.a.
Ligands
GTX ×2
PG4
Waters ×228
HEADER    TRANSFERASE                             30-NOV-05   2C80
TITLE     STRUCTURE OF SH28GST IN COMPLEX WITH S-HEXYL GLUTATHIONE
CAVEAT     2C80    MET B 114 C-ALPHA IS PLANAR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE 28 KDA;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: GST 28, GST CLASS-SIGMA;
COMPND   5 EC: 2.5.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SCHISTOSOMA HAEMATOBIUM;
SOURCE   3 ORGANISM_COMMON: BLOOD FLUKE;
SOURCE   4 ORGANISM_TAXID: 6185;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-23D
KEYWDS    SIGMA CLASS GST, DETOXIFICATION, GLUTATHIONE, PROSTAGLANDIN
KEYWDS   2 D2 SYNTHASE, INHIBITOR, TRANSFERASE, ANTIGEN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.BAIOCCO,L.J.GOURLAY,F.ANGELUCCI,A.BELLELLI,A.E.MIELE,
AUTHOR   2 M.BRUNORI
REVDAT   4   08-MAY-13 2C80    1       TITLE  CAVEAT SOURCE REMARK
REVDAT   4 2                           VERSN  HETNAM HETSYN FORMUL
REVDAT   3   24-FEB-09 2C80    1       VERSN
REVDAT   2   12-JUL-06 2C80    1       JRNL
REVDAT   1   21-JUN-06 2C80    0
JRNL        AUTH   P.BAIOCCO,L.J.GOURLAY,F.ANGELUCCI,J.FONTAINE,
JRNL        AUTH 2 M.HERVE,A.E.MIELE,F.TROTTEIN,M.BRUNORI,A.BELLELLI
JRNL        TITL   PROBING THE MECHANISM OF GSH ACTIVATION IN
JRNL        TITL 2 SCHISTOSOMA HAEMATOBIUM GLUTATHIONE-S-TRANSFERASE
JRNL        TITL 3 BY SITE-DIRECTED MUTAGENESIS AND X-RAY
JRNL        TITL 4 CRYSTALLOGRAPHY.
JRNL        REF    J.MOL.BIOL.                   V. 360   678 2006
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   16777141
JRNL        DOI    10.1016/J.JMB.2006.05.040
REMARK   2
REMARK   2 RESOLUTION.    2.3  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.14
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0
REMARK   3   NUMBER OF REFLECTIONS             : 18295
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 + TEST SET) : 0.191
REMARK   3   R VALUE            (WORKING SET) : 0.188
REMARK   3   FREE R VALUE                     : 0.246
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 985
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.31
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1281
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.95
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2000
REMARK   3   BIN FREE R VALUE SET COUNT          : 71
REMARK   3   BIN FREE R VALUE                    : 0.3260
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3373
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 65
REMARK   3   SOLVENT ATOMS            : 228
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.86
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.06000
REMARK   3    B22 (A**2) : 0.06000
REMARK   3    B33 (A**2) : -0.09000
REMARK   3    B12 (A**2) : 0.03000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.439
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.258
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.178
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.140
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3483 ; 0.008 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4689 ; 1.186 ; 1.988
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   414 ; 5.317 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   151 ;30.170 ;24.172
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   655 ;14.402 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;23.352 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   520 ; 0.084 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2540 ; 0.003 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1695 ; 0.195 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2356 ; 0.302 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   237 ; 0.148 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    47 ; 0.194 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    22 ; 0.177 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2144 ; 0.452 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3367 ; 0.786 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1509 ; 1.138 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1322 ; 1.813 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2C80 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-NOV-05.
REMARK 100 THE PDBE ID CODE IS EBI-26605.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-APR-05
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 6.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ELETTRA
REMARK 200  BEAMLINE                       : 5.2R
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
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   : 18295
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : 0.12000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 6.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1OE7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%PEG3350, 0.2M MES PH 6.0,
REMARK 280  5MM BETA-MERCAPTOETHANOL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       94.30067
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       47.15033
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: 4830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.2 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 400
REMARK 400 COMPOUND
REMARK 400  CENTRAL ROLE IN THE PARASITE DETOXIFICATION SYSTEM
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     THR A     2
REMARK 465     GLY A     3
REMARK 465     MET B     1
REMARK 465     THR B     2
REMARK 465     GLY B     3
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    MET B 114   CA    MET B 114   CB     -0.320
REMARK 500    GLU B 117   CA    GLU B 117   CB      0.713
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    MET B 114   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES
REMARK 500    MET B 114   CB  -  CA  -  C   ANGL. DEV. =  14.9 DEGREES
REMARK 500    MET B 114   N   -  CA  -  CB  ANGL. DEV. =  12.1 DEGREES
REMARK 500    GLU B 118   N   -  CA  -  C   ANGL. DEV. =  17.3 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    GLU A  70       95.99     72.20
REMARK 500    GLU A 118      -76.13    -22.00
REMARK 500    ASP A 174      106.20   -160.78
REMARK 500    ALA A 207       66.96     96.98
REMARK 500    ARG B  14      -71.12    -74.96
REMARK 500    GLU B  70       96.26     70.06
REMARK 500    GLU B 117       30.36    -63.24
REMARK 500    GLU B 118       10.12    174.61
REMARK 500    GLU B 119      -81.82     36.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLU B  118     GLU B  119                   42.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    MET B 114         4.7      L          L   EXPECTING SP3
REMARK 500    GLU B 118        23.8      L          L   OUTSIDE RANGE
REMARK 500    GLU B 119        22.4      L          L   OUTSIDE RANGE
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 GTX A1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTX B1213
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C8U   RELATED DB: PDB
REMARK 900  STRUCTURE OF R21Q MUTANT OF SH28GST
REMARK 900 RELATED ID: 2CA8   RELATED DB: PDB
REMARK 900  STRUCTURE OF SH28GST IN COMPLEX WITH GSH AT PH 6.0
REMARK 900 RELATED ID: 2CAI   RELATED DB: PDB
REMARK 900  STRUCTURE OF GLUTATHIONE-S-TRANSFERASE MUTANT,
REMARK 900  R21L, FROM SCHISTOSOMA HAEMATOBIUM
REMARK 900 RELATED ID: 2CAQ   RELATED DB: PDB
REMARK 900  STRUCTURE OF R21L MUTANT OF SH28GST IN
REMARK 900  COMPLEX WITH GSH
DBREF  2C80 A    1   211  UNP    P30113   GST28_SCHBO      1    211
DBREF  2C80 B    1   211  UNP    P30113   GST28_SCHBO      1    211
SEQRES   1 A  211  MET THR GLY ASP HIS ILE LYS VAL ILE TYR PHE ASN GLY
SEQRES   2 A  211  ARG GLY ARG ALA GLU SER ILE ARG MET THR LEU VAL ALA
SEQRES   3 A  211  ALA GLY VAL ASN TYR GLU ASP GLU ARG ILE SER PHE GLN
SEQRES   4 A  211  ASP TRP PRO LYS ILE LYS PRO THR ILE PRO GLY GLY ARG
SEQRES   5 A  211  LEU PRO ALA VAL LYS ILE THR ASP ASN HIS GLY HIS VAL
SEQRES   6 A  211  LYS TRP MET VAL GLU SER LEU ALA ILE ALA ARG TYR MET
SEQRES   7 A  211  ALA LYS LYS HIS HIS MET MET GLY GLY THR GLU GLU GLU
SEQRES   8 A  211  TYR TYR ASN VAL GLU LYS LEU ILE GLY GLN ALA GLU ASP
SEQRES   9 A  211  LEU GLU HIS GLU TYR TYR LYS THR LEU MET LYS PRO GLU
SEQRES  10 A  211  GLU GLU LYS GLN LYS ILE ILE LYS GLU ILE LEU ASN GLY
SEQRES  11 A  211  LYS VAL PRO VAL LEU LEU ASP ILE ILE CYS GLU SER LEU
SEQRES  12 A  211  LYS ALA SER THR GLY LYS LEU ALA VAL GLY ASP LYS VAL
SEQRES  13 A  211  THR LEU ALA ASP LEU VAL LEU ILE ALA VAL ILE ASP HIS
SEQRES  14 A  211  VAL THR ASP LEU ASP LYS GLU PHE LEU THR GLY LYS TYR
SEQRES  15 A  211  PRO GLU ILE HIS LYS HIS ARG GLU ASN LEU LEU ALA SER
SEQRES  16 A  211  SER PRO ARG LEU ALA LYS TYR LEU SER ASP ARG ALA ALA
SEQRES  17 A  211  THR PRO PHE
SEQRES   1 B  211  MET THR GLY ASP HIS ILE LYS VAL ILE TYR PHE ASN GLY
SEQRES   2 B  211  ARG GLY ARG ALA GLU SER ILE ARG MET THR LEU VAL ALA
SEQRES   3 B  211  ALA GLY VAL ASN TYR GLU ASP GLU ARG ILE SER PHE GLN
SEQRES   4 B  211  ASP TRP PRO LYS ILE LYS PRO THR ILE PRO GLY GLY ARG
SEQRES   5 B  211  LEU PRO ALA VAL LYS ILE THR ASP ASN HIS GLY HIS VAL
SEQRES   6 B  211  LYS TRP MET VAL GLU SER LEU ALA ILE ALA ARG TYR MET
SEQRES   7 B  211  ALA LYS LYS HIS HIS MET MET GLY GLY THR GLU GLU GLU
SEQRES   8 B  211  TYR TYR ASN VAL GLU LYS LEU ILE GLY GLN ALA GLU ASP
SEQRES   9 B  211  LEU GLU HIS GLU TYR TYR LYS THR LEU MET LYS PRO GLU
SEQRES  10 B  211  GLU GLU LYS GLN LYS ILE ILE LYS GLU ILE LEU ASN GLY
SEQRES  11 B  211  LYS VAL PRO VAL LEU LEU ASP ILE ILE CYS GLU SER LEU
SEQRES  12 B  211  LYS ALA SER THR GLY LYS LEU ALA VAL GLY ASP LYS VAL
SEQRES  13 B  211  THR LEU ALA ASP LEU VAL LEU ILE ALA VAL ILE ASP HIS
SEQRES  14 B  211  VAL THR ASP LEU ASP LYS GLU PHE LEU THR GLY LYS TYR
SEQRES  15 B  211  PRO GLU ILE HIS LYS HIS ARG GLU ASN LEU LEU ALA SER
SEQRES  16 B  211  SER PRO ARG LEU ALA LYS TYR LEU SER ASP ARG ALA ALA
SEQRES  17 B  211  THR PRO PHE
HET    GTX  A1212      26
HET    PG4  B1212      13
HET    GTX  B1213      26
HETNAM     GTX S-HEXYLGLUTATHIONE
HETNAM     PG4 TETRAETHYLENE GLYCOL
FORMUL   3  GTX    2(C16 H30 N3 O6 S 1+)
FORMUL   4  PG4    C8 H18 O5
FORMUL   6  HOH   *228(H2 O)
HELIX    1   1 ARG A   14  ARG A   16  5                                   3
HELIX    2   2 ALA A   17  GLY A   28  1                                  12
HELIX    3   3 ASP A   40  LYS A   45  1                                   6
HELIX    4   4 PRO A   46  ILE A   48  5                                   3
HELIX    5   5 GLU A   70  HIS A   82  1                                  13
HELIX    6   6 THR A   88  LYS A  111  1                                  24
HELIX    7   7 PRO A  116  GLY A  130  1                                  15
HELIX    8   8 GLY A  130  ALA A  145  1                                  16
HELIX    9   9 THR A  157  ASP A  174  1                                  18
HELIX   10  10 TYR A  182  SER A  196  1                                  15
HELIX   11  11 SER A  196  ARG A  206  1                                  11
HELIX   12  12 ALA B   17  GLY B   28  1                                  12
HELIX   13  13 ASP B   40  LYS B   45  1                                   6
HELIX   14  14 PRO B   46  ILE B   48  5                                   3
HELIX   15  15 GLU B   70  HIS B   82  1                                  13
HELIX   16  16 THR B   88  LYS B  111  1                                  24
HELIX   17  17 GLU B  119  GLY B  130  1                                  12
HELIX   18  18 GLY B  130  ALA B  145  1                                  16
HELIX   19  19 THR B  157  ASP B  174  1                                  18
HELIX   20  20 TYR B  182  SER B  196  1                                  15
HELIX   21  21 SER B  196  ASP B  205  1                                  10
SHEET    1  AA 4 GLU A  32  ILE A  36  0
SHEET    2  AA 4 HIS A   5  PHE A  11  1  O  ILE A   6   N  GLU A  32
SHEET    3  AA 4 ALA A  55  THR A  59 -1  O  ALA A  55   N  ILE A   9
SHEET    4  AA 4 VAL A  65  VAL A  69 -1  O  LYS A  66   N  ILE A  58
SHEET    1  BA 4 GLU B  32  ILE B  36  0
SHEET    2  BA 4 HIS B   5  PHE B  11  1  O  ILE B   6   N  GLU B  32
SHEET    3  BA 4 ALA B  55  THR B  59 -1  O  ALA B  55   N  ILE B   9
SHEET    4  BA 4 VAL B  65  VAL B  69 -1  O  LYS B  66   N  ILE B  58
CISPEP   1 LEU A   53    PRO A   54          0         2.99
CISPEP   2 ARG A  206    ALA A  207          0        27.63
CISPEP   3 LEU B   53    PRO B   54          0         0.85
SITE     1 AC1 14 TYR A  10  ARG A  16  TRP A  41  LYS A  45
SITE     2 AC1 14 ARG A  52  LEU A  53  PRO A  54  GLU A  70
SITE     3 AC1 14 SER A  71  TYR A 110  HOH A2106  HOH A2107
SITE     4 AC1 14 ASP B 104  HOH B2059
SITE     1 AC2  7 LYS A  80  GLY A  86  TYR A  92  LYS B  80
SITE     2 AC2  7 GLY B  86  THR B  88  TYR B  92
SITE     1 AC3 18 ASP A 104  TYR B  10  GLY B  15  ARG B  16
SITE     2 AC3 18 TRP B  41  LYS B  45  ARG B  52  LEU B  53
SITE     3 AC3 18 PRO B  54  GLU B  70  SER B  71  TYR B 110
SITE     4 AC3 18 LEU B 113  PHE B 211  HOH B2118  HOH B2119
SITE     5 AC3 18 HOH B2120  HOH B2121
CRYST1   52.832   52.832  141.451  90.00  90.00 120.00 P 32          6
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      0.018928  0.010928  0.000000        0.00000
SCALE2      0.000000  0.021856  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007070        0.00000
      
PROCHECK
Go to PROCHECK summary
 References