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PDBsum entry 1v0x

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Oxidoreductase PDB id
1v0x
Jmol
Contents
Protein chain
604 a.a.
HEADER    OXIDOREDUCTASE                          02-APR-04   1V0X
TITLE     THEORETICAL MODEL STRUCTURE OF HUMAN CYCLOOXGENASE-2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CYCLOOXYGENASE-2, COX-2, PGH SYNTHASE 2,
COMPND   5 PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2, PGHS-2, PHS II,
COMPND   6 PROSTAGLANDIN H2 SYNTHASE 2;
COMPND   7 EC: 1.14.99.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN
KEYWDS    OXIDOREDUCTASE, DIOXYGENASE, PEROXIDASE, GLYCOPROTEIN,
KEYWDS   2 PROSTAGLANDIN BIOSYNTHESIS, HEME, IRON
EXPDTA    THEORETICAL MODEL
AUTHOR    S.MAHANTA,P.K.SARMA,A.K.BURAGOHAIN
REVDAT   1   06-APR-04 1V0X    0
JRNL        AUTH   S.MAHANTA,P.K.SARMA,A.K.BURAGOHAIN
JRNL        TITL   THEORETICAL MODEL STRUCTURE OF HUMAN
JRNL        TITL 2 CYCLOOXGENASE-2
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   R.A.GUPTA,R.N.CUBOIS
REMARK   1  TITL   COLORECTAL CANCER PREVENTION AND TREATMENT BY
REMARK   1  TITL 2 INHIBITION OF CYCLOOXYGENASE-2
REMARK   1  REF    NAT.REV. CANCER               V.   1    11 2001
REMARK   1  REFN   ASTM NRCAC4  UK ISSN 1474-175X
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : NULL
REMARK   3   AUTHORS     : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1V0X COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI  ON  2-APR-2004.
REMARK 100 THE EBI ID CODE IS EBI-14906.
REMARK 220
REMARK 220 EXPERIMENTAL DETAILS
REMARK 220  EXPERIMENT TYPE                : THEORETICAL MODELLING
REMARK 220
REMARK 220 REMARK: NULL
REMARK 225
REMARK 225 THEORETICAL MODEL
REMARK 225 THE COORDINATES IN THIS ENTRY REPRESENT A MODEL STRUCTURE.
REMARK 225 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT CRYST1 AND
REMARK 225 SCALE RECORDS BE INCLUDED, BUT THE VALUES ON THESE
REMARK 225 RECORDS ARE MEANINGLESS.
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    GLN A 194   CG  -  CD  -  OE1 ANGL. DEV. =-75.5 DEGREES
REMARK 500    GLN A 194   CG  -  CD  -  NE2 ANGL. DEV. =-23.4 DEGREES
REMARK 500    GLN A 313   CG  -  CD  -  OE1 ANGL. DEV. =-76.0 DEGREES
REMARK 500    GLN A 313   CG  -  CD  -  NE2 ANGL. DEV. =-23.3 DEGREES
REMARK 500    GLN A 336   CG  -  CD  -  OE1 ANGL. DEV. =-75.9 DEGREES
REMARK 500    GLN A 336   CG  -  CD  -  NE2 ANGL. DEV. =-23.4 DEGREES
REMARK 500    ASN A 354   CB  -  CG  -  OD1 ANGL. DEV. =-76.1 DEGREES
REMARK 500    ASN A 354   CB  -  CG  -  ND2 ANGL. DEV. =-23.1 DEGREES
REMARK 500    ASN A 450   CB  -  CG  -  OD1 ANGL. DEV. =-75.7 DEGREES
REMARK 500    ASN A 450   CB  -  CG  -  ND2 ANGL. DEV. =-23.1 DEGREES
DBREF  1V0X A    1   604  UNP    P35354   PGH2_HUMAN       1    604
SEQRES   1 A  604  MET LEU ALA ARG ALA LEU LEU LEU CYS ALA VAL LEU ALA
SEQRES   2 A  604  LEU SER HIS THR ALA ASN PRO CYS CYS SER HIS PRO CYS
SEQRES   3 A  604  GLN ASN ARG GLY VAL CYS MET SER VAL GLY PHE ASP GLN
SEQRES   4 A  604  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU
SEQRES   5 A  604  ASN CYS SER THR PRO GLU PHE LEU THR ARG ILE LYS LEU
SEQRES   6 A  604  PHE LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU
SEQRES   7 A  604  THR HIS PHE LYS GLY PHE TRP ASN VAL VAL ASN ASN ILE
SEQRES   8 A  604  PRO PHE LEU ARG ASN ALA ILE MET SER TYR VAL LEU THR
SEQRES   9 A  604  SER ARG SER HIS LEU ILE ASP SER PRO PRO THR TYR ASN
SEQRES  10 A  604  ALA ASP TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN
SEQRES  11 A  604  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL PRO ASP
SEQRES  12 A  604  ASP CYS PRO THR PRO LEU GLY VAL LYS GLY LYS LYS GLN
SEQRES  13 A  604  LEU PRO ASP SER ASN GLU ILE VAL GLU LYS LEU LEU LEU
SEQRES  14 A  604  ARG ARG LYS PHE ILE PRO ASP PRO GLN GLY SER ASN MET
SEQRES  15 A  604  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE
SEQRES  16 A  604  PHE LYS THR ASP HIS LYS ARG GLY PRO ALA PHE THR ASN
SEQRES  17 A  604  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY
SEQRES  18 A  604  GLU THR LEU ALA ARG GLN ARG LYS LEU ARG LEU PHE LYS
SEQRES  19 A  604  ASP GLY LYS MET LYS TYR GLN ILE ILE ASP GLY GLU MET
SEQRES  20 A  604  TYR PRO PRO THR VAL LYS ASP THR GLN ALA GLU MET ILE
SEQRES  21 A  604  TYR PRO PRO GLN VAL PRO GLU HIS LEU ARG PHE ALA VAL
SEQRES  22 A  604  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET
SEQRES  23 A  604  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS
SEQRES  24 A  604  ASP VAL LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU
SEQRES  25 A  604  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU
SEQRES  26 A  604  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU
SEQRES  27 A  604  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU
SEQRES  28 A  604  LEU PHE ASN LYS GLN PHE GLN TYR GLN ASN ARG ILE ALA
SEQRES  29 A  604  ALA GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU
SEQRES  30 A  604  PRO ASP THR PHE GLN ILE HIS ASP GLN LYS TYR ASN TYR
SEQRES  31 A  604  GLN GLN PHE ILE TYR ASN ASN SER ILE LEU LEU GLU HIS
SEQRES  32 A  604  GLY ILE THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE
SEQRES  33 A  604  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO PRO ALA
SEQRES  34 A  604  VAL GLN LYS VAL SER GLN ALA SER ILE ASP GLN SER ARG
SEQRES  35 A  604  GLN MET LYS TYR GLN SER PHE ASN GLU TYR ARG LYS ARG
SEQRES  36 A  604  PHE MET LEU LYS PRO TYR GLU SER PHE GLU GLU LEU THR
SEQRES  37 A  604  GLY GLU LYS GLU MET SER ALA GLU LEU GLU ALA LEU TYR
SEQRES  38 A  604  GLY ASP ILE ASP ALA VAL GLU LEU TYR PRO ALA LEU LEU
SEQRES  39 A  604  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR
SEQRES  40 A  604  MET VAL GLU VAL GLY ALA PRO PHE SER LEU LYS GLY LEU
SEQRES  41 A  604  MET GLY ASN VAL ILE CYS SER PRO ALA TYR TRP LYS PRO
SEQRES  42 A  604  SER THR PHE GLY GLY GLU VAL GLY PHE GLN ILE ILE ASN
SEQRES  43 A  604  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS
SEQRES  44 A  604  GLY CYS PRO PHE THR SER PHE SER VAL PRO ASP PRO GLU
SEQRES  45 A  604  LEU ILE LYS THR VAL THR ILE ASN ALA SER SER SER ARG
SEQRES  46 A  604  SER GLY LEU ASP ASP ILE ASN PRO THR VAL LEU LEU LYS
SEQRES  47 A  604  GLU ARG SER THR GLU LEU
HELIX    1   1 GLU A   58  LYS A   68  1                                  11
HELIX    2   2 THR A   70  HIS A   80  1                                  11
HELIX    3   3 PHE A   81  ILE A   91  1                                  11
HELIX    4   4 ILE A   91  HIS A  108  1                                  18
HELIX    5   5 SER A  124  ASN A  130  1                                   7
HELIX    6   6 ASP A  159  LEU A  168  1                                  10
HELIX    7   7 ASN A  181  HIS A  193  1                                  13
HELIX    8   8 LEU A  216  GLY A  221  1                                   6
HELIX    9   9 THR A  223  ARG A  231  1                                   9
HELIX   10  10 THR A  251  GLN A  256  1                                   6
HELIX   11  11 PRO A  266  ARG A  270  5                                   5
HELIX   12  12 GLN A  275  LEU A  280  5                                   6
HELIX   13  13 VAL A  281  HIS A  306  1                                  26
HELIX   14  14 GLY A  310  ASP A  333  1                                  24
HELIX   15  15 ASP A  333  GLY A  340  1                                   8
HELIX   16  16 ASP A  348  PHE A  353  5                                   6
HELIX   17  17 ALA A  364  TYR A  371  1                                   8
HELIX   18  18 TRP A  373  LEU A  377  5                                   5
HELIX   19  19 ASN A  389  ILE A  394  1                                   6
HELIX   20  20 ASN A  396  GLY A  404  1                                   9
HELIX   21  21 GLY A  404  GLN A  415  1                                  12
HELIX   22  22 VAL A  430  MET A  444  1                                  15
HELIX   23  23 SER A  448  PHE A  456  1                                   9
HELIX   24  24 SER A  463  GLY A  469  1                                   7
HELIX   25  25 LYS A  471  GLY A  482  1                                  12
HELIX   26  26 GLU A  488  GLU A  496  1                                   9
HELIX   27  27 GLY A  505  GLY A  522  1                                  18
HELIX   28  28 ASN A  523  SER A  527  5                                   5
HELIX   29  29 LYS A  532  GLY A  537  5                                   6
HELIX   30  30 GLY A  538  THR A  547  1                                  10
HELIX   31  31 SER A  549  VAL A  558  1                                  10
SHEET    1  AA 2 VAL A  31  SER A  34  0
SHEET    2  AA 2 TYR A  40  ASP A  43 -1  O  LYS A  41   N  MET A  33
SHEET    1  AB 2 PHE A  49  TYR A  50  0
SHEET    2  AB 2 THR A  56  PRO A  57 -1  O  THR A  56   N  TYR A  50
SHEET    1  AC 2 GLN A 241  ILE A 243  0
SHEET    2  AC 2 GLU A 246  TYR A 248 -1  O  GLU A 246   N  ILE A 243
SHEET    1  AD 2 PHE A 381  ILE A 383  0
SHEET    2  AD 2 GLN A 386  TYR A 388 -1  O  GLN A 386   N  ILE A 383
SSBOND   1 CYS A   21    CYS A   32
SSBOND   2 CYS A   22    CYS A  145
SSBOND   3 CYS A   26    CYS A   42
SSBOND   4 CYS A   44    CYS A   54
SSBOND   5 CYS A  555    CYS A  561
CISPEP   1 SER A  112    PRO A  113          0         2.87
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1
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      1.000000  0.000000  0.000000        0.00000
SCALE2      0.000000  1.000000  0.000000        0.00000
SCALE3      0.000000  0.000000  1.000000        0.00000
      
PROCHECK
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