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PDBsum entry 1qrg

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Lyase PDB id
1qrg
Jmol
Contents
Protein chain
206 a.a. *
Metals
_ZN
Waters ×75
* Residue conservation analysis
HEADER    LYASE                                   13-JUN-99   1QRG
TITLE     A CLOSER LOOK AND THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HIGH
TITLE    2 RESOLUTION CRYSTALLOGRAPHIC STUDIES OF THE CARBONIC ANHYDRASE FROM
TITLE    3 METHANOSARCINA THERMOPHILA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: METHANOSARCINA THERMOPHILA;
SOURCE   3 ORGANISM_TAXID: 2210;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    BETA-HELIX, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.M.IVERSON,B.E.ALBER,C.KISKER,J.G.FERRY,D.C.REES
REVDAT   6   13-JUL-11 1QRG    1       VERSN
REVDAT   5   24-FEB-09 1QRG    1       VERSN
REVDAT   4   01-APR-03 1QRG    1       JRNL
REVDAT   3   18-APR-01 1QRG    1       LINK
REVDAT   2   27-SEP-00 1QRG    1       JRNL   REMARK SOURCE DBREF
REVDAT   1   25-JUN-99 1QRG    0
JRNL        AUTH   T.M.IVERSON,B.E.ALBER,C.KISKER,J.G.FERRY,D.C.REES
JRNL        TITL   A CLOSER LOOK AT THE ACTIVE SITE OF GAMMA-CLASS CARBONIC
JRNL        TITL 2 ANHYDRASES: HIGH-RESOLUTION CRYSTALLOGRAPHIC STUDIES OF THE
JRNL        TITL 3 CARBONIC ANHYDRASE FROM METHANOSARCINA THERMOPHILA.
JRNL        REF    BIOCHEMISTRY                  V.  39  9222 2000
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   10924115
JRNL        DOI    10.1021/BI000204S
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   C.KISKER,H.SCHINDELIN,B.ALBER,J.FERRY,D.REES
REMARK   1  TITL   A LEFT-HANDED BETA-HELIX REVEALED BY THE CRYSTAL STRUCTURE
REMARK   1  TITL 2 OF A CARBONIC ANHYDRASE FROM THE ARCHAEON METHANOSARCINA
REMARK   1  TITL 3 THERMOPHILA
REMARK   1  REF    EMBO J.                       V.  15  2323 1996
REMARK   1  REFN                   ISSN 0261-4189
REMARK   2
REMARK   2 RESOLUTION.    1.72 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.72
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 19889
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191
REMARK   3   R VALUE            (WORKING SET) : 0.189
REMARK   3   FREE R VALUE                     : 0.227
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1134
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1541
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 75
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 18.00
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1QRG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-99.
REMARK 100 THE RCSB ID CODE IS RCSB009178.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 22-APR-98
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL7-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08
REMARK 200  MONOCHROMATOR                  : NULL
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, CCP4 (TRUNCATE)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19889
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.720
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 6.400
REMARK 200  R MERGE                    (I) : 0.09700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.78
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.24000
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: ISOMORPHOUS 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   (%): 40.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, AMMONIUM SULFATE, PH 5.8,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290       5555   Z,X,Y
REMARK 290       6555   Z+1/2,-X+1/2,-Y
REMARK 290       7555   -Z+1/2,-X,Y+1/2
REMARK 290       8555   -Z,X+1/2,-Y+1/2
REMARK 290       9555   Y,Z,X
REMARK 290      10555   -Y,Z+1/2,-X+1/2
REMARK 290      11555   Y+1/2,-Z+1/2,-X
REMARK 290      12555   -Y+1/2,-Z,X+1/2
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       41.32100
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.32100
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.32100
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       41.32100
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       41.32100
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.32100
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       41.32100
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       41.32100
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       41.32100
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       41.32100
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       41.32100
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       41.32100
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       41.32100
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       41.32100
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       41.32100
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       41.32100
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       41.32100
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       41.32100
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -154.0 KCAL/MOL
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 350   BIOMT1   2  0.000000  0.000000 -1.000000       82.64200
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000       41.32100
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000      123.96300
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000      -41.32100
REMARK 350   BIOMT2   3  0.000000  0.000000 -1.000000      123.96300
REMARK 350   BIOMT3   3 -1.000000  0.000000  0.000000       82.64200
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     GLN A     1
REMARK 465     GLU A     2
REMARK 465     ILE A     3
REMARK 465     THR A     4
REMARK 465     VAL A     5
REMARK 465     ASP A     6
REMARK 465     GLU A     7
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     GLU A  22    CG   CD   OE1  OE2
REMARK 470     ASN A  87    CG   OD1
REMARK 470     GLU A  91    CG   CD   OE1  OE2
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    ARG A  12   CD  -  NE  -  CZ  ANGL. DEV. =  29.4 DEGREES
REMARK 500    MET A  64   CA  -  CB  -  CG  ANGL. DEV. =  12.0 DEGREES
REMARK 500    HIS A  81   CG  -  ND1 -  CE1 ANGL. DEV. =   7.5 DEGREES
REMARK 500    HIS A 117   CE1 -  NE2 -  CD2 ANGL. DEV. =   7.1 DEGREES
REMARK 500    HIS A 122   CE1 -  NE2 -  CD2 ANGL. DEV. =   7.5 DEGREES
REMARK 500    ASP A 130   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG A 153   CG  -  CD  -  NE  ANGL. DEV. = -16.7 DEGREES
REMARK 500    ARG A 153   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A 153   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.3 DEGREES
REMARK 500    ARG A 165   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    TYR A 191   CB  -  CG  -  CD1 ANGL. DEV. =   3.9 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    SER A  60       78.45   -107.78
REMARK 500    GLU A  62      -90.62   -116.00
REMARK 500    GLU A  88      -56.09     -3.64
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                              ZN A 214  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 288   O
REMARK 620 2 HOH A 289   O    69.1
REMARK 620 3 HIS A 122   NE2  92.6 119.2
REMARK 620 4 HIS A  81   ND1  91.2 120.8 116.8
REMARK 620 5 HIS A 117   NE2 160.4  91.8 101.0  95.1
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 214
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1THJ   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE
REMARK 900 RELATED ID: 1QQ0   RELATED DB: PDB
REMARK 900 COBALT SUBSTITUTED CARBONIC ANHYDRASE
REMARK 900 RELATED ID: 1QQE   RELATED DB: PDB
REMARK 900 COBALT SUBSTITUTED CARBONIC ANHYDRASE + BICARBONATE
REMARK 900 RELATED ID: 1QRF   RELATED DB: PDB
REMARK 900 COBALT SUBSTITUTED CARBONIC ANHYDRASE + SULFATE
REMARK 900 RELATED ID: 1QRL   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE + BICARBONATE
REMARK 900 RELATED ID: 1QRM   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE + SULFATE
DBREF  1QRG A    1   213  UNP    P40881   CAH_METTE       35    247
SEQRES   1 A  213  GLN GLU ILE THR VAL ASP GLU PHE SER ASN ILE ARG GLU
SEQRES   2 A  213  ASN PRO VAL THR PRO TRP ASN PRO GLU PRO SER ALA PRO
SEQRES   3 A  213  VAL ILE ASP PRO THR ALA TYR ILE ASP PRO GLN ALA SER
SEQRES   4 A  213  VAL ILE GLY GLU VAL THR ILE GLY ALA ASN VAL MET VAL
SEQRES   5 A  213  SER PRO MET ALA SER ILE ARG SER ASP GLU GLY MET PRO
SEQRES   6 A  213  ILE PHE VAL GLY ASP ARG SER ASN VAL GLN ASP GLY VAL
SEQRES   7 A  213  VAL LEU HIS ALA LEU GLU THR ILE ASN GLU GLU GLY GLU
SEQRES   8 A  213  PRO ILE GLU ASP ASN ILE VAL GLU VAL ASP GLY LYS GLU
SEQRES   9 A  213  TYR ALA VAL TYR ILE GLY ASN ASN VAL SER LEU ALA HIS
SEQRES  10 A  213  GLN SER GLN VAL HIS GLY PRO ALA ALA VAL GLY ASP ASP
SEQRES  11 A  213  THR PHE ILE GLY MET GLN ALA PHE VAL PHE LYS SER LYS
SEQRES  12 A  213  VAL GLY ASN ASN CYS VAL LEU GLU PRO ARG SER ALA ALA
SEQRES  13 A  213  ILE GLY VAL THR ILE PRO ASP GLY ARG TYR ILE PRO ALA
SEQRES  14 A  213  GLY MET VAL VAL THR SER GLN ALA GLU ALA ASP LYS LEU
SEQRES  15 A  213  PRO GLU VAL THR ASP ASP TYR ALA TYR SER HIS THR ASN
SEQRES  16 A  213  GLU ALA VAL VAL TYR VAL ASN VAL HIS LEU ALA GLU GLY
SEQRES  17 A  213  TYR LYS GLU THR SER
HET     ZN  A 214       1
HETNAM      ZN ZINC ION
FORMUL   2   ZN    ZN 2+
FORMUL   3  HOH   *75(H2 O)
HELIX    1   1 GLU A   94  ILE A   97  5                                   4
HELIX    2   2 SER A  175  LYS A  181  1                                   7
HELIX    3   3 HIS A  193  GLU A  211  1                                  19
SHEET    1   A 8 ASN A  10  ARG A  12  0
SHEET    2   A 8 SER A  39  GLY A  42  1  N  VAL A  40   O  ASN A  10
SHEET    3   A 8 ALA A  56  SER A  60  1  O  ALA A  56   N  SER A  39
SHEET    4   A 8 VAL A  78  HIS A  81  1  O  VAL A  78   N  SER A  57
SHEET    5   A 8 SER A 119  GLY A 123  1  O  SER A 119   N  VAL A  79
SHEET    6   A 8 ALA A 137  LYS A 141  1  O  ALA A 137   N  GLN A 120
SHEET    7   A 8 SER A 154  GLY A 158  1  O  SER A 154   N  PHE A 138
SHEET    8   A 8 MET A 171  VAL A 173  1  O  MET A 171   N  ALA A 155
SHEET    1   B 7 VAL A  27  ASP A  29  0
SHEET    2   B 7 GLU A  43  GLY A  47  1  O  VAL A  44   N  VAL A  27
SHEET    3   B 7 PRO A  65  GLY A  69  1  N  ILE A  66   O  GLU A  43
SHEET    4   B 7 ALA A 106  GLY A 110  1  N  VAL A 107   O  PRO A  65
SHEET    5   B 7 PRO A 124  GLY A 128  1  N  ALA A 125   O  ALA A 106
SHEET    6   B 7 SER A 142  GLY A 145  1  N  SER A 142   O  PRO A 124
SHEET    7   B 7 VAL A 159  ILE A 161  1  O  VAL A 159   N  LYS A 143
SHEET    1   C 7 TYR A  33  ASP A  35  0
SHEET    2   C 7 VAL A  50  SER A  53  1  O  VAL A  50   N  TYR A  33
SHEET    3   C 7 SER A  72  GLN A  75  1  O  SER A  72   N  MET A  51
SHEET    4   C 7 VAL A 113  ALA A 116  1  O  VAL A 113   N  ASN A  73
SHEET    5   C 7 THR A 131  GLY A 134  1  O  THR A 131   N  SER A 114
SHEET    6   C 7 CYS A 148  GLU A 151  1  O  CYS A 148   N  PHE A 132
SHEET    7   C 7 ARG A 165  ILE A 167  1  O  ARG A 165   N  VAL A 149
SHEET    1   D 2 VAL A  98  VAL A 100  0
SHEET    2   D 2 LYS A 103  TYR A 105 -1  O  LYS A 103   N  VAL A 100
LINK        ZN    ZN A 214                 O   HOH A 288     1555   1555  2.16
LINK        ZN    ZN A 214                 O   HOH A 289     1555   1555  2.03
LINK        ZN    ZN A 214                 NE2 HIS A 122     1555   1555  2.23
LINK        ZN    ZN A 214                 ND1 HIS A  81     1555   1555  2.31
LINK        ZN    ZN A 214                 NE2 HIS A 117     1555   8656  2.19
CISPEP   1 MET A   64    PRO A   65          0        -0.13
CISPEP   2 GLY A  123    PRO A  124          0         0.64
SITE     1 AC1  5 HIS A  81  HIS A 117  HIS A 122  HOH A 288
SITE     2 AC1  5 HOH A 289
CRYST1   82.642   82.642   82.642  90.00  90.00  90.00 P 21 3       12
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      0.012100  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012100  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012100        0.00000
      
PROCHECK
Go to PROCHECK summary
 References