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PDBsum entry 4ee0

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Top Page protein ligands metals Protein-protein interface(s) links
Isomerase/isomerase inhibitor PDB id
4ee0
Jmol
Contents
Protein chain
194 a.a.
Ligands
0O4 ×2
GSF ×2
Metals
_MG
Waters ×310
HEADER    ISOMERASE/ISOMERASE INHIBITOR           28-MAR-12   4EE0
TITLE     CRYSTAL STRUCTURE OF HH-PGDS WITH WATER DISPLACING INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: H-PGDS, GST CLASS-SIGMA, GLUTATHIONE S-TRANSFERASE,
COMPND   5 GLUTATHIONE-DEPENDENT PGD SYNTHASE, GLUTATHIONE-REQUIRING
COMPND   6 PROSTAGLANDIN D SYNTHASE, PROSTAGLANDIN-H2 D-ISOMERASE;
COMPND   7 EC: 5.3.99.2, 2.5.1.18;
COMPND   8 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: GSTS, HPGDS, PGDS, PTGDS2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    INHIBITOR, SOLVENT REPLACEMENT, ISOMERASE-ISOMERASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.E.DAY,A.THORARENSEN,J.I.TRUJILLO
REVDAT   1   18-JUL-12 4EE0    0
JRNL        AUTH   J.I.TRUJILLO,J.R.KIEFER,W.HUANG,J.E.DAY,J.MOON,G.M.JEROME,
JRNL        AUTH 2 C.P.BONO,C.M.KORNMEIER,M.L.WILLIAMS,C.KUHN,G.R.RENNIE,
JRNL        AUTH 3 T.A.WYNN,C.P.CARRON,A.THORARENSEN
JRNL        TITL   INVESTIGATION OF THE BINDING POCKET OF HUMAN HEMATOPOIETIC
JRNL        TITL 2 PROSTAGLANDIN (PG) D2 SYNTHASE (HH-PGDS): A TALE OF TWO
JRNL        TITL 3 WATERS.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  22  3795 2012
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   22546671
JRNL        DOI    10.1016/J.BMCL.2012.04.004
REMARK   2
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
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) : 1.75
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.73
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9
REMARK   3   NUMBER OF REFLECTIONS             : 37441
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) : 0.197
REMARK   3   R VALUE            (WORKING SET) : 0.196
REMARK   3   FREE R VALUE                     : 0.223
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 1929
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) : 1.74
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.78
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2171
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.71
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940
REMARK   3   BIN FREE R VALUE SET COUNT          : 121
REMARK   3   BIN FREE R VALUE                    : 0.3590
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3209
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 99
REMARK   3   SOLVENT ATOMS            : 307
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.71
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.05000
REMARK   3    B22 (A**2) : -0.08000
REMARK   3    B33 (A**2) : 0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.58000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.139
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.124
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.085
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.541
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3413 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  2304 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4632 ; 1.062 ; 1.989
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5605 ; 0.828 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   384 ; 4.865 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   161 ;34.267 ;24.099
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   568 ;12.334 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;13.069 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   504 ; 0.059 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3694 ; 0.005 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   693 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  1948 ; 0.408 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   773 ; 0.091 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3165 ; 0.764 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1465 ; 1.271 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1467 ; 2.036 ; 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  : 2
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     1        A   199
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4239  -0.1560  21.4692
REMARK   3    T TENSOR
REMARK   3      T11:   0.0158 T22:   0.0162
REMARK   3      T33:   0.0168 T12:  -0.0047
REMARK   3      T13:   0.0136 T23:  -0.0134
REMARK   3    L TENSOR
REMARK   3      L11:   1.2878 L22:   1.7809
REMARK   3      L33:   1.8519 L12:   0.0235
REMARK   3      L13:   0.3220 L23:   0.1750
REMARK   3    S TENSOR
REMARK   3      S11:   0.0060 S12:  -0.0117 S13:   0.0210
REMARK   3      S21:   0.0147 S22:   0.0176 S23:  -0.0450
REMARK   3      S31:   0.0415 S32:   0.0753 S33:  -0.0236
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     1        B   199
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9707 -19.6920   6.8058
REMARK   3    T TENSOR
REMARK   3      T11:   0.0142 T22:   0.0067
REMARK   3      T33:   0.0070 T12:  -0.0027
REMARK   3      T13:   0.0095 T23:  -0.0030
REMARK   3    L TENSOR
REMARK   3      L11:   1.8847 L22:   1.3264
REMARK   3      L33:   1.1513 L12:  -0.5905
REMARK   3      L13:   0.4528 L23:   0.0090
REMARK   3    S TENSOR
REMARK   3      S11:   0.0321 S12:   0.0993 S13:   0.0202
REMARK   3      S21:  -0.0736 S22:  -0.0294 S23:   0.0022
REMARK   3      S31:  -0.0079 S32:   0.0356 S33:  -0.0027
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 4EE0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071498.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
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 MICROMAX-007
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : OSMIC MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39455
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06600
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       38.93800
REMARK 290   SMTRY3   2  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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: 4090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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     HIS A     1
REMARK 465     GLN A    36
REMARK 465     ALA A    37
REMARK 465     ASP A    38
REMARK 465     TRP A    39
REMARK 465     GLU B    35
REMARK 465     GLN B    36
REMARK 465     LYS B   107
REMARK 465     LYS B   108
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     HIS B   1    CG   ND1  CD2  CE1  NE2
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  63      107.96     74.09
REMARK 500    GLN B  63      106.86     75.29
REMARK 500    ASP B 110      -68.65     73.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 201  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 323   O
REMARK 620 2 HOH A 318   O    90.9
REMARK 620 3 HOH B 356   O    99.1 170.0
REMARK 620 4 HOH B 349   O   173.7  83.2  86.8
REMARK 620 5 HOH B 317   O    87.5  92.3  87.5  90.5
REMARK 620 6 HOH A 334   O    92.1  94.9  85.5  90.6 172.9
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0O4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSF A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0O4 B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSF B 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EDZ   RELATED DB: PDB
REMARK 900 RELATED ID: 4EDY   RELATED DB: PDB
DBREF  4EE0 A    2   199  UNP    O60760   HPGDS_HUMAN      2    199
DBREF  4EE0 B    2   199  UNP    O60760   HPGDS_HUMAN      2    199
SEQADV 4EE0 HIS A    1  UNP  O60760              EXPRESSION TAG
SEQADV 4EE0 HIS B    1  UNP  O60760              EXPRESSION TAG
SEQRES   1 A  199  HIS PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG GLY
SEQRES   2 A  199  ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU ASP
SEQRES   3 A  199  ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP TRP
SEQRES   4 A  199  PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE PRO
SEQRES   5 A  199  ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER LEU
SEQRES   6 A  199  ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU ALA
SEQRES   7 A  199  GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA ILE
SEQRES   8 A  199  VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO TRP
SEQRES   9 A  199  ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE ASN
SEQRES  10 A  199  GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN ASP
SEQRES  11 A  199  LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE GLY
SEQRES  12 A  199  ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE CYS
SEQRES  13 A  199  SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU ASP
SEQRES  14 A  199  ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL GLN
SEQRES  15 A  199  ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG PRO
SEQRES  16 A  199  GLN THR LYS LEU
SEQRES   1 B  199  HIS PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG GLY
SEQRES   2 B  199  ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU ASP
SEQRES   3 B  199  ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP TRP
SEQRES   4 B  199  PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE PRO
SEQRES   5 B  199  ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER LEU
SEQRES   6 B  199  ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU ALA
SEQRES   7 B  199  GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA ILE
SEQRES   8 B  199  VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO TRP
SEQRES   9 B  199  ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE ASN
SEQRES  10 B  199  GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN ASP
SEQRES  11 B  199  LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE GLY
SEQRES  12 B  199  ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE CYS
SEQRES  13 B  199  SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU ASP
SEQRES  14 B  199  ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL GLN
SEQRES  15 B  199  ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG PRO
SEQRES  16 B  199  GLN THR LYS LEU
HET     MG  A 201       1
HET    0O4  A 202      27
HET    GSF  A 203      44
HET    0O4  B 201      27
HET    GSF  B 202      22
HETNAM      MG MAGNESIUM ION
HETNAM     0O4 4-(ISOQUINOLIN-1-YL)-N-[2-(MORPHOLIN-4-YL)
HETNAM   2 0O4  ETHYL]BENZAMIDE
HETNAM     GSF L-GAMMA-GLUTAMYL-3-SULFINO-L-ALANYLGLYCINE
HETSYN     GSF GLUTATHIONE SULFINATE
FORMUL   3   MG    MG 2+
FORMUL   4  0O4    2(C22 H23 N3 O2)
FORMUL   5  GSF    2(C10 H17 N3 O8 S)
FORMUL   8  HOH   *307(H2 O)
HELIX    1   1 ALA A   15  LEU A   25  1                                  11
HELIX    2   2 GLU A   41  LEU A   46  5                                   6
HELIX    3   3 GLN A   63  LYS A   73  1                                  11
HELIX    4   4 THR A   81  CYS A  101  1                                  21
HELIX    5   5 LYS A  108  TYR A  122  1                                  15
HELIX    6   6 TYR A  122  GLY A  136  1                                  15
HELIX    7   7 THR A  147  LYS A  164  1                                  18
HELIX    8   8 HIS A  171  ILE A  184  1                                  14
HELIX    9   9 ILE A  184  ARG A  194  1                                  11
HELIX   10  10 ARG B   12  ARG B   14  5                                   3
HELIX   11  11 ALA B   15  ASP B   26  1                                  12
HELIX   12  12 ASP B   38  SER B   44  1                                   7
HELIX   13  13 GLN B   63  LYS B   73  1                                  11
HELIX   14  14 THR B   81  PHE B  102  1                                  22
HELIX   15  15 ASP B  110  ASN B  123  1                                  14
HELIX   16  16 ASN B  123  GLY B  136  1                                  14
HELIX   17  17 THR B  147  LYS B  164  1                                  18
HELIX   18  18 HIS B  171  ILE B  184  1                                  14
HELIX   19  19 ILE B  184  ARG B  194  1                                  11
SHEET    1   A 4 GLU A  30  ILE A  34  0
SHEET    2   A 4 TYR A   4  PHE A   9  1  N  LEU A   6   O  GLU A  30
SHEET    3   A 4 ILE A  53  VAL A  56 -1  O  GLU A  55   N  LYS A   5
SHEET    4   A 4 LEU A  59  HIS A  62 -1  O  LEU A  59   N  VAL A  56
SHEET    1   B 4 GLU B  30  ILE B  34  0
SHEET    2   B 4 TYR B   4  PHE B   9  1  N  TYR B   4   O  GLU B  30
SHEET    3   B 4 ILE B  53  VAL B  56 -1  O  GLU B  55   N  LYS B   5
SHEET    4   B 4 LEU B  59  HIS B  62 -1  O  LEU B  61   N  LEU B  54
LINK        MG    MG A 201                 O   HOH A 323     1555   1555  2.00
LINK        MG    MG A 201                 O   HOH A 318     1555   1555  2.01
LINK        MG    MG A 201                 O   HOH B 356     1555   1555  2.06
LINK        MG    MG A 201                 O   HOH B 349     1555   1555  2.08
LINK        MG    MG A 201                 O   HOH B 317     1555   1555  2.10
LINK        MG    MG A 201                 O   HOH A 334     1555   1555  2.14
CISPEP   1 ILE A   34    GLU A   35          0         4.98
CISPEP   2 ILE A   51    PRO A   52          0         7.17
CISPEP   3 ILE B   51    PRO B   52          0         9.87
SITE     1 AC1  6 HOH A 318  HOH A 323  HOH A 334  HOH B 317
SITE     2 AC1  6 HOH B 349  HOH B 356
SITE     1 AC2 10 MET A  11  GLY A  13  ARG A  14  ASP A  96
SITE     2 AC2 10 MET A  99  TRP A 104  TYR A 152  LEU A 199
SITE     3 AC2 10 GSF A 203  HOH A 320
SITE     1 AC3 17 TYR A   8  PHE A   9  ARG A  14  LYS A  43
SITE     2 AC3 17 GLY A  49  LYS A  50  ILE A  51  PRO A  52
SITE     3 AC3 17 GLN A  63  SER A  64  0O4 A 202  HOH A 326
SITE     4 AC3 17 HOH A 327  HOH A 355  HOH A 357  HOH A 398
SITE     5 AC3 17 ASP B  97
SITE     1 AC4 13 PHE B   9  MET B  11  GLY B  13  ARG B  14
SITE     2 AC4 13 ASP B  96  MET B  99  SER B 100  TRP B 104
SITE     3 AC4 13 TYR B 152  GSF B 202  HOH B 344  HOH B 430
SITE     4 AC4 13 HOH B 453
SITE     1 AC5 16 ASP A  97  TYR B   8  PHE B   9  ARG B  14
SITE     2 AC5 16 TRP B  39  LYS B  43  LYS B  50  ILE B  51
SITE     3 AC5 16 GLN B  63  SER B  64  0O4 B 201  HOH B 318
SITE     4 AC5 16 HOH B 321  HOH B 322  HOH B 325  HOH B 427
CRYST1   48.612   77.876   52.560  90.00  91.39  90.00 P 1 21 1      4
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      0.020571  0.000000  0.000499        0.00000
SCALE2      0.000000  0.012841  0.000000        0.00000
SCALE3      0.000000  0.000000  0.019031        0.00000
      
PROCHECK
Go to PROCHECK summary
 References