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PDBsum entry 1bnq

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Lyase PDB id
1bnq
Jmol
Contents
Protein chain
256 a.a.
Ligands
AL4
Metals
_HG
_ZN
Waters ×57
HEADER    LYASE                                   30-JUL-98   1BNQ
TITLE     CARBONIC ANHYDRASE II INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 4.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 CELL: ERYTHROCYTES;
SOURCE   6 CELLULAR_LOCATION: CYTOPLASM
KEYWDS    CO2 HYDRATION, ZINC ENZYME, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.A.BORIACK-SJODIN,S.ZEITLIN,D.W.CHRISTIANSON
REVDAT   2   24-FEB-09 1BNQ    1       VERSN
REVDAT   1   15-JUN-99 1BNQ    0
JRNL        AUTH   P.A.BORIACK-SJODIN,S.ZEITLIN,H.H.CHEN,L.CRENSHAW,
JRNL        AUTH 2 S.GROSS,A.DANTANARAYANA,P.DELGADO,J.A.MAY,T.DEAN,
JRNL        AUTH 3 D.W.CHRISTIANSON
JRNL        TITL   STRUCTURAL ANALYSIS OF INHIBITOR BINDING TO HUMAN
JRNL        TITL 2 CARBONIC ANHYDRASE II.
JRNL        REF    PROTEIN SCI.                  V.   7  2483 1998
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   9865942
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.40 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) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.50
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 77.5
REMARK   3   NUMBER OF REFLECTIONS             : 7301
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.143
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
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            : 2640
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 24
REMARK   3   SOLVENT ATOMS            : 57
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) : 0.014
REMARK   3   BOND ANGLES            (DEGREES) : 3.10
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.91
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.20
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
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 : NULL
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  : PARAM19X.PRO
REMARK   3  PARAMETER FILE  2  : PARAM19XAL4623.PRO
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOP19X.PRO
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : TOP19XAL4623.PRO
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1BNQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
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        : JUN-93
REMARK 200  TEMPERATURE           (KELVIN) : 298
REMARK 200  PH                             : 10.0
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          : RIGAKU RUH2R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NI FILTER
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : BUDDHA
REMARK 200  DATA SCALING SOFTWARE          : PROTEIN
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7686
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 6.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 77.5
REMARK 200  DATA REDUNDANCY                : 2.000
REMARK 200  R MERGE                    (I) : 0.10200
REMARK 200  R SYM                      (I) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: 1CBA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 43.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 10.0
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       20.85000
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 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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     SER A     2
REMARK 465     HIS A     3
REMARK 465     LYS A   261
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     PHE A 260    O
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    HIS A  10   NE2   HIS A  10   CD2    -0.076
REMARK 500    HIS A  15   NE2   HIS A  15   CD2    -0.069
REMARK 500    HIS A  17   NE2   HIS A  17   CD2    -0.067
REMARK 500    HIS A  94   NE2   HIS A  94   CD2    -0.074
REMARK 500    HIS A 107   NE2   HIS A 107   CD2    -0.072
REMARK 500    HIS A 119   NE2   HIS A 119   CD2    -0.076
REMARK 500    HIS A 122   NE2   HIS A 122   CD2    -0.068
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    TRP A   5   CD1 -  CG  -  CD2 ANGL. DEV. =   6.8 DEGREES
REMARK 500    TRP A   5   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES
REMARK 500    TRP A  16   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    TRP A  16   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ARG A  27   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    TYR A  40   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ARG A  58   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500    ARG A  58   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.2 DEGREES
REMARK 500    TRP A  97   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    TRP A  97   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES
REMARK 500    TRP A 123   CD1 -  CG  -  CD2 ANGL. DEV. =   7.1 DEGREES
REMARK 500    TRP A 123   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.5 DEGREES
REMARK 500    ARG A 182   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    TRP A 192   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    TRP A 192   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    TYR A 194   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    TRP A 209   CD1 -  CG  -  CD2 ANGL. DEV. =   7.7 DEGREES
REMARK 500    TRP A 209   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.4 DEGREES
REMARK 500    TRP A 245   CD1 -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES
REMARK 500    TRP A 245   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG A 246   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 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    ASN A  11       19.02   -147.97
REMARK 500    ARG A  27       55.29   -140.57
REMARK 500    LYS A 111       -3.60     69.37
REMARK 500    PHE A 176       64.63   -154.88
REMARK 500    ASN A 244       53.62   -100.36
REMARK 500    LYS A 252       74.95     22.65
REMARK 500    ASN A 253       43.79     79.36
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 289        DISTANCE =  5.56 ANGSTROMS
REMARK 525    HOH A 299        DISTANCE =  5.13 ANGSTROMS
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                              ZN A 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 103.2
REMARK 620 3 HIS A 119   ND1 114.9  95.1
REMARK 620 4 AL4 A 555   N21 105.6 117.0 120.0
REMARK 620 5 AL4 A 555   S1   95.3 142.7 106.2  25.7
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              HG A 362  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 206   SG
REMARK 620 2 GLN A 137   O    82.6
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE WITH CATALYTIC ZINC ION
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 362
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 262
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AL4 A 555
DBREF  1BNQ A    2   261  UNP    P00918   CAH2_HUMAN       1    259
SEQRES   1 A  259  SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU
SEQRES   2 A  259  HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG
SEQRES   3 A  259  GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR
SEQRES   4 A  259  ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN
SEQRES   5 A  259  ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE
SEQRES   6 A  259  ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU
SEQRES   7 A  259  LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN
SEQRES   8 A  259  PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER
SEQRES   9 A  259  GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU
SEQRES  10 A  259  HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY
SEQRES  11 A  259  LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY
SEQRES  12 A  259  ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN
SEQRES  13 A  259  LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY
SEQRES  14 A  259  LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU
SEQRES  15 A  259  LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER
SEQRES  16 A  259  LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE
SEQRES  17 A  259  VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL
SEQRES  18 A  259  LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU
SEQRES  19 A  259  PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN
SEQRES  20 A  259  PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     HG  A 362       1
HET     ZN  A 262       1
HET    AL4  A 555      22
HETNAM      HG MERCURY (II) ION
HETNAM      ZN ZINC ION
HETNAM     AL4 (R)-4-ETHYLAMINO-3,4-DIHYDRO-2-(2-METHOYLETHYL)-2H-
HETNAM   2 AL4  THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE-1,1-DIOXIDE
HETSYN     AL4 AL4623
FORMUL   2   HG    HG 2+
FORMUL   3   ZN    ZN 2+
FORMUL   4  AL4    C11 H19 N3 O5 S3
FORMUL   5  HOH   *57(H2 O)
HELIX    1   1 PRO A   13  LYS A   18  5                                   6
HELIX    2   2 PRO A   21  LYS A   24  5                                   4
HELIX    3   3 THR A  125  TYR A  128  5                                   3
HELIX    4   4 PHE A  131  GLN A  136  1                                   6
HELIX    5   5 PRO A  155  ILE A  167  1                                  13
HELIX    6   6 PRO A  181  LEU A  184  5                                   4
HELIX    7   7 SER A  220  LYS A  228  1                                   9
SHEET    1   A 2 LEU A  47  SER A  50  0
SHEET    2   A 2 VAL A  78  GLY A  81 -1  N  LYS A  80   O  SER A  48
SHEET    1   B 3 SER A 173  ASP A 175  0
SHEET    2   B 3 SER A  56  ASN A  61 -1  N  ILE A  59   O  ALA A 174
SHEET    3   B 3 PHE A  66  PHE A  70 -1  N  GLU A  69   O  LEU A  57
SHEET    1   C 5 TYR A 191  GLY A 196  0
SHEET    2   C 5 VAL A 207  LEU A 212 -1  N  VAL A 211   O  TRP A 192
SHEET    3   C 5 LEU A 141  LEU A 148  1  N  LEU A 141   O  THR A 208
SHEET    4   C 5 ALA A 116  ASN A 124 -1  N  HIS A 122   O  ALA A 142
SHEET    5   C 5 TYR A  88  TRP A  97 -1  N  HIS A  96   O  GLU A 117
SHEET    1   D 2 LEU A 148  VAL A 150  0
SHEET    2   D 2 ILE A 216  VAL A 218  1  N  ILE A 216   O  LYS A 149
LINK        ZN    ZN A 262                 NE2 HIS A  94     1555   1555  2.17
LINK        ZN    ZN A 262                 NE2 HIS A  96     1555   1555  2.04
LINK        ZN    ZN A 262                 ND1 HIS A 119     1555   1555  2.04
LINK        ZN    ZN A 262                 N21 AL4 A 555     1555   1555  1.94
LINK        HG    HG A 362                 SG  CYS A 206     1555   1555  2.42
LINK        HG    HG A 362                 O   GLN A 137     1555   1555  3.29
LINK        ZN    ZN A 262                 S1  AL4 A 555     1555   1555  2.97
CISPEP   1 SER A   29    PRO A   30          0        -2.46
CISPEP   2 PRO A  201    PRO A  202          0         3.58
SITE     1  ZN  3 HIS A  94  HIS A  96  HIS A 119
SITE     1 AC1  4 VAL A 135  GLN A 137  GLU A 205  CYS A 206
SITE     1 AC2  4 HIS A  94  HIS A  96  HIS A 119  AL4 A 555
SITE     1 AC3 13 TRP A   5  HIS A  64  GLN A  92  HIS A  94
SITE     2 AC3 13 HIS A  96  HIS A 119  VAL A 121  PHE A 131
SITE     3 AC3 13 LEU A 198  THR A 199  THR A 200   ZN A 262
SITE     4 AC3 13 HOH A 271
CRYST1   42.700   41.700   73.000  90.00 104.60  90.00 P 1 21 1      2
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      0.023419  0.000000  0.006100        0.00000
SCALE2      0.000000  0.023981  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014156        0.00000
      
PROCHECK
Go to PROCHECK summary
 References