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PDBsum entry 2vva

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Lyase PDB id
2vva
Jmol
Contents
Protein chain
258 a.a.
Ligands
SO4
CO2 ×2
GOL ×2
Metals
_ZN
Waters ×350
HEADER    LYASE                                   04-JUN-08   2VVA
TITLE     HUMAN CARBONIC ANHYDRASE IN COMPLEX WITH CO2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: X;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE II, CARBONATE DEHYDRATASE II,
COMPND   5  CARBONIC ANHYDRASE C, CAC, CA-II;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    METAL-BINDING, CARBON DIOXIDE, DISEASE MUTATION, SUBSTRATE
KEYWDS   2 BINDING, CARBONIC ANHYDRASE, ZINC, LYASE, CYTOPLASM,
KEYWDS   3 ACETYLATION, POLYMORPHISM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.SJOEBLOM,M.POLENTARUTTI,K.DJINOVIC-CARUGO
REVDAT   1   14-JUL-09 2VVA    0
JRNL        AUTH   B.SJOBLOM,M.POLENTARUTTI,K.DJINOVIC-CARUGO
JRNL        TITL   STRUCTURAL STUDY OF X-RAY INDUCED ACTIVATION OF
JRNL        TITL 2 CARBONIC ANHYDRASE.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 106 10609 2009
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   19520834
JRNL        DOI    10.1073/PNAS.0904184106
REMARK   2
REMARK   2 RESOLUTION.    1.56 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 1.56
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.19
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.1
REMARK   3   NUMBER OF REFLECTIONS             : 30130
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) : 0.156
REMARK   3   R VALUE            (WORKING SET) : 0.153
REMARK   3   FREE R VALUE                     : 0.200
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1614
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) : 1.56
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.60
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2250
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1680
REMARK   3   BIN FREE R VALUE SET COUNT          : 120
REMARK   3   BIN FREE R VALUE                    : 0.2180
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2108
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 12
REMARK   3   SOLVENT ATOMS            : 362
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.79
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.35000
REMARK   3    B22 (A**2) : -0.28000
REMARK   3    B33 (A**2) : -0.13000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.13000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.088
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.094
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.048
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.249
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2197 ; 0.017 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  1508 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2987 ; 1.682 ; 1.952
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3697 ; 0.965 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   273 ; 6.551 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   101 ;34.450 ;24.653
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   367 ;11.710 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;23.914 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   309 ; 0.105 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2451 ; 0.009 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   433 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   417 ; 0.196 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1613 ; 0.195 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1047 ; 0.180 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1091 ; 0.087 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   239 ; 0.144 ; 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):    14 ; 0.199 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    44 ; 0.263 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    27 ; 0.130 ; 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):  1695 ; 1.354 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2142 ; 1.660 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1033 ; 2.633 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   841 ; 3.488 ; 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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 2VVA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  05-JUN-08.
REMARK 100 THE PDBE ID CODE IS EBI-36382.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
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                  : SI(111)
REMARK 200  OPTICS                         : MIRROR
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   : 35235
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.56
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.90
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.5
REMARK 200  DATA REDUNDANCY                : 4.7
REMARK 200  R MERGE                    (I) : 0.04
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) : 1.56
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.64
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.5
REMARK 200  R MERGE FOR SHELL          (I) : 0.11
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: PDB ENTRY 2CBA
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M (NH4)2(SO4). 0.1 M TRIS
REMARK 280  PH = 8.5
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       20.78850
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 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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     MET X     1
REMARK 465     SER X     2
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    ASP X 165   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 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 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    ARG X  27       50.15   -143.43
REMARK 500    ASN X 244       46.74    -89.45
REMARK 500    LYS X 252     -135.96     57.37
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 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 X1267  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS X  96   NE2
REMARK 620 2 HIS X 119   ND1 100.2
REMARK 620 3 HIS X  94   NE2 108.9 115.3
REMARK 620 4 HOH X2350   O   110.3 113.3 108.6
REMARK 620 N                    1     2     3
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 X1262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO2 X1263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO2 X1264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL X1265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL X1266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN X1267
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OKL   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKL
REMARK 900   INHIBITOR 5-DIMETHYLAMINO-NAPHTHALENE-1-
REMARK 900  SULFONAMIDE
REMARK 900 RELATED ID: 1I9Q   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH
REMARK 900  4-(AMINOSULFONYL)-N-[(3,4,5-TRIFLUOROPHENYL
REMARK 900  )METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1ZFQ   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II IN COMPLEX WITH
REMARK 900  ETHOXZOLAMIDPHENOLEAS SULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 1IF7   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH (R)-N
REMARK 900  -(3-INDOL-1-YL-2-METHYL-PROPYL)-4-
REMARK 900  SULFAMOYL-BENZAMIDE
REMARK 900 RELATED ID: 1CAM   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH THR 199
REMARK 900  REPLACED BY ALA (T199A) COMPLEX WITH
REMARK 900  BICARBONATE
REMARK 900 RELATED ID: 1T9N   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH
REMARK 900  ENVIRONMENT ON H+TRANSFER IN HUMAN CARBONIC
REMARK 900   ANHYDRASE II
REMARK 900 RELATED ID: 1CNW   RELATED DB: PDB
REMARK 900  MOL_ID: 1; MOLECULE: CARBONIC ANHYDRASE II;
REMARK 900  CHAIN: NULL; SYNONYM: CARBONATE DEHYDRATASE,
REMARK 900  HCA II; EC: 4.2.1.1; HETEROGEN:
REMARK 900  ETHYLAMINOCARBONYLBENZENESULFONAMIDE
REMARK 900 RELATED ID: 1OKN   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKN
REMARK 900   INHIBITOR 4-SULFONAMIDE-[1-(4-N-(5-
REMARK 900  FLUORESCEIN THIOUREA)BUTANE)]
REMARK 900 RELATED ID: 1F2W   RELATED DB: PDB
REMARK 900  THE MECHANISM OF CYANAMIDE HYDRATION CATALYZED
REMARK 900   BY CARBONIC ANHYDRASE II REVEALED BY
REMARK 900  CRYOGENIC X-RAY DIFFRACTION
REMARK 900 RELATED ID: 1G52   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH 4-(
REMARK 900  AMINOSULFONYL)-N-[(2,3-DIFLUOROPHENYL)METHYL
REMARK 900  ]-BENZAMIDE
REMARK 900 RELATED ID: 2H4N   RELATED DB: PDB
REMARK 900  H94N CARBONIC ANHYDRASE II COMPLEXED WITH
REMARK 900  ACETAZOLAMIDE
REMARK 900 RELATED ID: 1BNM   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1BNQ   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1CNH   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE,
REMARK 900  HCA II, CA2) MUTANT WITH GLN 92 REPLACED
REMARK 900  BY GLU (Q92E)
REMARK 900 RELATED ID: 1XEV   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE
REMARK 900   II IN A NEWCRYSTAL FORM
REMARK 900 RELATED ID: 1UGC   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II [HCAII] MUTANT
REMARK 900  WITH ALA 65 REPLACED BY HIS (A65H)
REMARK 900 RELATED ID: 1UGG   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II[HCAII] MUTANT
REMARK 900  WITH ALA 65 REPLACED BY SER (A65S) -
REMARK 900  ORTHORHOMBIC FORM
REMARK 900 RELATED ID: 1IF9   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH N-[2-(
REMARK 900  1H-INDOL-5-YL)-BUTYL]-4-SULFAMOYL-
REMARK 900  BENZAMIDE
REMARK 900 RELATED ID: 1G53   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH 4-(
REMARK 900  AMINOSULFONYL)-N-[(2,6-DIFLUOROPHENYL)METHYL
REMARK 900  ]-BENZAMIDE
REMARK 900 RELATED ID: 1FQM   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93I
REMARK 900  /F95M/W97VCARBONIC ANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 1CA2   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II)
REMARK 900 RELATED ID: 1FQL   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F95M
REMARK 900  /W97V CARBONICANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 1CAL   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH THR 199
REMARK 900  REPLACED BY ALA (T199A)
REMARK 900 RELATED ID: 1I9N   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH
REMARK 900  4-(AMINOSULFONYL)-N-[(2,5-DIFLUOROPHENYL)
REMARK 900  METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1G4O   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH
REMARK 900  4-(AMINOSULFONYL)-N-PHENYLMETHYLBENZAMIDE
REMARK 900 RELATED ID: 2CBA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (50 MM TRIS, 3 M
REMARK 900  AMMONIUM SULFATE, PH 7.8)
REMARK 900 RELATED ID: 1YDC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE)(
REMARK 900  HCA II) MUTANT WITH LEU 198 REPLACED BY
REMARK 900  PHE (L198F)
REMARK 900 RELATED ID: 1LZV   RELATED DB: PDB
REMARK 900  SITE-SPECIFIC MUTANT (TYR7 REPLACED WITH HIS
REMARK 900  ) OF HUMANCARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1CCS   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE,
REMARK 900  HCA II) MUTANT WITH THR 199 REPLACED BY
REMARK 900  ASP (T199D)
REMARK 900 RELATED ID: 1BNV   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1FQR   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND
REMARK 900  F93I/F95M/W97VCARBONIC ANHYDRASE (CAII)
REMARK 900  VARIANT
REMARK 900 RELATED ID: 1RZB   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II WITH ZINC REPLACED BY
REMARK 900   BY COBALT(II) AT PH 6.0
REMARK 900 RELATED ID: 1A42   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH
REMARK 900  BRINZOLAMIDE
REMARK 900 RELATED ID: 1TH9   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH
REMARK 900  ENVIRONMENT ON H+TRANSFER IN HUMAN CARBONIC
REMARK 900   ANHYDRASE II
REMARK 900 RELATED ID: 1ZSB   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT E117Q, TRANSITION
REMARK 900   STATE ANALOGUE ACETAZOLAMIDE
REMARK 900 RELATED ID: 1CNB   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE,
REMARK 900  HCA II) MUTANT WITH HIS 94 REPLACED BY
REMARK 900  CYS (H94C) COMPLEXED WITH BETA-MERCAPTOETHANOL
REMARK 900   (BME)
REMARK 900 RELATED ID: 1I8Z   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH AL-6629
REMARK 900   2H-THIENO[3,2-E]-1,2-THIAZINE-6-
REMARK 900  SULFONAMIDE, 2-(3-METHOXYPHENYL)-3-(4-
REMARK 900  MORPHOLINYL)-, 1,1-DIOXIDE
REMARK 900 RELATED ID: 1HED   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) MUTANT WITH LEU 198 REPLACED BY
REMARK 900  ALA (L198A)
REMARK 900 RELATED ID: 1G48   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH
REMARK 900  4-(AMINOSULFONYL)-N-[(2,6-DIFLUOROPHENYL)
REMARK 900  METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1LG5   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF THE HCA II
REMARK 900  MUTANT T199P INCOMPLEX WITH BETA-
REMARK 900  MERCAPTOETHANOL
REMARK 900 RELATED ID: 1BV3   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH
REMARK 900  UREA
REMARK 900 RELATED ID: 1G0F   RELATED DB: PDB
REMARK 900  SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH
REMARK 900  ALA) OF HUMANCARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1UGD   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II[HCAII] MUTANT
REMARK 900  WITH ALA 65 REPLACED BY SER (A65S)
REMARK 900 RELATED ID: 1TG3   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH
REMARK 900  ENVIRONMENT ON H+TRANSFER IN HUMAN CARBONIC
REMARK 900   ANHYDRASE II
REMARK 900 RELATED ID: 1CVC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH HIS 94
REMARK 900  REPLACED BY ASP (H94D)
REMARK 900 RELATED ID: 1YO0   RELATED DB: PDB
REMARK 900  PROTON TRANSFER FROM HIS200 IN HUMAN
REMARK 900  CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1I90   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH AL-8520
REMARK 900   2H-THIENO[3,2-E]-1,2-THIAZINE-6-
REMARK 900  SULFONAMIDE, 4-AMINO-3,4-DIHYDRO-2-(3-
REMARK 900  METHOXYPROPYL)-, 1,1-DIOXIDE, (R)
REMARK 900 RELATED ID: 1HVA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH HIS 94
REMARK 900  REPLACED BY CYS (H94C)
REMARK 900 RELATED ID: 1FSN   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF METAL-FREE F93S
REMARK 900  /F95L/W97MCARBONIC ANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 1UGB   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II[HCAII] MUTANT
REMARK 900  WITH ALA 65 REPLACED BY GLY (A65G)
REMARK 900 RELATED ID: 1RZE   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II WITH ZINC REPLACED BY
REMARK 900   NICKEL(II)
REMARK 900 RELATED ID: 1Z9Y   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II IN COMPLEX WITH
REMARK 900  FUROSEMIDE ASSULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 2FMZ   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE ACTIVATORS. ACTIVATION OF
REMARK 900  ISOFORMS I, II,IV, VA, VII AND XIV WITH
REMARK 900   L- AND D- PHENYLALANINE,STRUCTURE WITH D-
REMARK 900  PHENYLALANINE.
REMARK 900 RELATED ID: 1CNK   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE,
REMARK 900  HCA II, CA2) MUTANT WITH GLN 92 REPLACED
REMARK 900  BY LEU (Q92L)
REMARK 900 RELATED ID: 1BN1   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1TEQ   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH
REMARK 900  ENVIRONMENT ON H+TRANSFER IN HUMAN CARBONIC
REMARK 900   ANHYDRASE II
REMARK 900 RELATED ID: 1RZA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II WITH ZINC REPLACED BY
REMARK 900   COBALT(II)
REMARK 900 RELATED ID: 1CCU   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE,
REMARK 900  HCA II) MUTANT WITH THR 199 REPLACED BY
REMARK 900  HIS (T199H)
REMARK 900 RELATED ID: 1I9L   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH
REMARK 900  4-(AMINOSULFONYL)-N-[(4-FLUOROPHENYL)METHYL]-
REMARK 900  BENZAMIDE
REMARK 900 RELATED ID: 2CBC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (50 MM TRIS, 3 M
REMARK 900  AMMONIUM SULFATE, 0.2 FORMATE, PH 7.6)
REMARK 900 RELATED ID: 1CVB   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (HCA II) MUTANT WITH
REMARK 900  THR 199 REPLACED BY VAL (T199V) (SULFATE-
REMARK 900  BOUND FORM)
REMARK 900 RELATED ID: 1G46   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH
REMARK 900  4-(AMINOSULFONYL)-N-[(2,3-DIFLUOROPHENYL)
REMARK 900  METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1CAO   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH HYDROGEN
REMARK 900  SULFIDE
REMARK 900 RELATED ID: 1FSQ   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND
REMARK 900  F93S/F95L/W97MCARBONIC ANHYDRASE (CAII)
REMARK 900  VARIANT
REMARK 900 RELATED ID: 6CA2   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) MUTANT WITH VAL 143 REPLACED WITH
REMARK 900   PHE (V143F)
REMARK 900 RELATED ID: 5CA2   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) (MUTANT WITH THR 200 REPLACED WITH
REMARK 900   SER) (T200S)
REMARK 900 RELATED ID: 1CAJ   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH GLU 106
REMARK 900  REPLACED BY ASP (E106D)
REMARK 900 RELATED ID: 1G1D   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH 4-(
REMARK 900  AMINOSULFONYL)-N-[(2-FLUOROPHENYL)METHYL]-
REMARK 900  BENZAMIDE
REMARK 900 RELATED ID: 2FOU   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH
REMARK 900  TWO-PRONGINHIBITORS
REMARK 900 RELATED ID: 1CVF   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE)(
REMARK 900  HCA II) MUTANT WITH HIS 94 REPLACED BY
REMARK 900  ALA (H94A)
REMARK 900 RELATED ID: 1LGD   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF HCA II MUTANT
REMARK 900   T199P INCOMPLEX WITH BICARBONATE
REMARK 900 RELATED ID: 1IF6   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH 3,5-
REMARK 900  DIFLUOROBENZENESULFONAMIDE
REMARK 900 RELATED ID: 1BN4   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1TEU   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH
REMARK 900  ENVIRONMENT ON H+TRANSFER IN HUMAN CARBONIC
REMARK 900   ANHYDRASE II
REMARK 900 RELATED ID: 1CRA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH 1,2,4-
REMARK 900  TRIAZOLE
REMARK 900 RELATED ID: 1ZE8   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II IN COMPLEX WITH A
REMARK 900  MEMBRANE-IMPERMEANTSULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 1IF4   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH 4-
REMARK 900  FLUOROBENZENESULFONAMIDE
REMARK 900 RELATED ID: 1HEA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) MUTANT WITH LEU 198 REPLACED BY
REMARK 900  ARG (L198R)
REMARK 900 RELATED ID: 1HCA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) (PH 6.5)
REMARK 900 RELATED ID: 1CAH   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (NATIVE ZINC REPLACED
REMARK 900  BY COBALT) COMPLEX WITH BICARBONATE
REMARK 900 RELATED ID: 1G4J   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH
REMARK 900  4-(AMINOSULFONYL)-N-[(2,3,4,5,6-
REMARK 900  PENTAFLUOROPHENYL)METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1RAZ   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH BROMIDE
REMARK 900 RELATED ID: 1KWQ   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH
REMARK 900  INHIBITOR 2000-07
REMARK 900 RELATED ID: 1CIM   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH THE
REMARK 900  INHIBITOR PTS
REMARK 900 RELATED ID: 1CVH   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE
REMARK 900  II, HCA II) MUTANT WITH HIS 96 REPLACED
REMARK 900  BY CYS (H96C)
REMARK 900 RELATED ID: 1CIN   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH THE
REMARK 900  INHIBITOR MTS
REMARK 900 RELATED ID: 1IF8   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH (S)-N
REMARK 900  -(3-INDOL-1-YL-2-METHYL-PROPYL)-4-
REMARK 900  SULFAMOYL-BENZAMIDE
REMARK 900 RELATED ID: 1I9M   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH
REMARK 900  4-(AMINOSULFONYL)-N-[(2,4-DIFLUOROPHENYL)
REMARK 900  METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1ZFK   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II IN COMPLEX WITH N-4
REMARK 900  -SULFONAMIDPHENYL-N'-4-METHYLBENZOSULFONYLUREASE
REMARK 900   AS SULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 1ZSA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT E117Q, APO FORM
REMARK 900 RELATED ID: 1FQN   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF METAL-FREE F93I
REMARK 900  /F95M/W97VCARBONIC ANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 1LG6   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF HCA II MUTANT
REMARK 900   T199P INCOMPLEX WITH THIOCYANATE
REMARK 900 RELATED ID: 1CNC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE,
REMARK 900  HCA II) MUTANT WITH HIS 94 REPLACED BY
REMARK 900  CYS (H94C) COMPLEXED WITH ZINC
REMARK 900 RELATED ID: 1UGA   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II[HCAII] MUTANT
REMARK 900  WITH ALA 65 REPLACED BY PHE (A65F)
REMARK 900 RELATED ID: 1BNN   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 2FOQ   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH
REMARK 900  TWO-PRONGINHIBITORS
REMARK 900 RELATED ID: 1TB0   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH
REMARK 900  ENVIRONMENT ON H+TRANSFER IN HUMAN CARBONIC
REMARK 900   ANHYDRASE II
REMARK 900 RELATED ID: 1CAI   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH GLU 106
REMARK 900  REPLACED BY ALA (E106A)
REMARK 900 RELATED ID: 2AX2   RELATED DB: PDB
REMARK 900  PRODUCTION AND X-RAY CRYSTALLOGRAPHIC ANALYSIS
REMARK 900   OF FULLYDEUTERATED HUMAN CARBONIC ANHYDRASE
REMARK 900  II
REMARK 900 RELATED ID: 1DCB   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) MUTANT WITH THR 199 REPLACED BY
REMARK 900  CYS (T199C)
REMARK 900 RELATED ID: 1CNX   RELATED DB: PDB
REMARK 900  MOL_ID: 1; MOLECULE: CARBONIC ANHYDRASE II;
REMARK 900  CHAIN: NULL; SYNONYM: CARBONATE DEHYDRATASE,
REMARK 900  HCA II; EC: 4.2.1.1; HETEROGEN:
REMARK 900  BENZENESULFONAMIDE
REMARK 900 RELATED ID: 4CAC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE FORM C (PH 6)
REMARK 900 RELATED ID: 5CAC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE FORM C COMPLEX WITH
REMARK 900  HYDROGEN SULFITE
REMARK 900 RELATED ID: 2HD6   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN CARBONIC
REMARK 900  ANHYDRASE II INCOMPLEX WITH A HYPOXIA-
REMARK 900  ACTIVATABLE SULFONAMIDE.
REMARK 900 RELATED ID: 1TTM   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH
REMARK 900  667-COUMATE
REMARK 900 RELATED ID: 1CAK   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH GLU 106
REMARK 900  REPLACED BY GLN (E106Q)
REMARK 900 RELATED ID: 1I9O   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH
REMARK 900  4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL
REMARK 900  )METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1CNI   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE,
REMARK 900  HCA II, CA2) MUTANT WITH GLN 92 REPLACED
REMARK 900  BY ALA (Q92A)
REMARK 900 RELATED ID: 1CAN   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH NITRATE
REMARK 900 RELATED ID: 2EU3   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH
REMARK 900   NOVEL INHIBITORS
REMARK 900 RELATED ID: 1YDA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE)(
REMARK 900  HCA II) MUTANT WITH LEU 198 REPLACED BY
REMARK 900  GLU (L198E) COMPLEXED WITH TRANSITION STATE
REMARK 900  ANALOG ACETAZOLAMIDE
REMARK 900 RELATED ID: 1YO2   RELATED DB: PDB
REMARK 900  PROTON TRANSFER FROM HIS200 IN HUMAN
REMARK 900  CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1EOU   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE
REMARK 900   II COMPLEXEDWITH AN ANTICONVULSANT SUGAR
REMARK 900  SULFAMATE
REMARK 900 RELATED ID: 1MUA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH PRO 202
REMARK 900  REPLACED BY ALA (P202A)
REMARK 900 RELATED ID: 2CA2   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) COMPLEX WITH THIOCYANATE ION
REMARK 900 RELATED ID: 1CCT   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE,
REMARK 900  HCA II) MUTANT WITH THR 199 REPLACED BY
REMARK 900  GLU (T199E)
REMARK 900 RELATED ID: 2ABE   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE ACTIVATORS: X-RAY CRYSTAL
REMARK 900  STRUCTURE OFTHE ADDUCT OF HUMAN ISOZYME II
REMARK 900  WITH L-HISTIDINE AS APLATFORM FOR THE
REMARK 900  DESIGN OF STRONGER ACTIVATORS
REMARK 900 RELATED ID: 1OQ5   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II IN COMPLEX WITH
REMARK 900  NANOMOLAR INHIBITOR
REMARK 900 RELATED ID: 1UGF   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II [HCAII] MUTANT
REMARK 900  WITH ALA 65 REPLACED BY THR (A65T)
REMARK 900 RELATED ID: 1RZC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II WITH ZINC REPLACED BY
REMARK 900   COPPER(II)
REMARK 900 RELATED ID: 1THK   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH
REMARK 900  ENVIRONMENT ON H+TRANSFER IN HUMAN CARBONIC
REMARK 900   ANHYDRASE II
REMARK 900 RELATED ID: 2CBE   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (50 MM TRIS, 3 M
REMARK 900  AMMONIUM SULFATE, 2MM DIPICOLINATE, PH 7.8)
REMARK 900 RELATED ID: 1KWR   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH
REMARK 900  INHIBITOR 0134-36
REMARK 900 RELATED ID: 1ZGF   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II IN COMPLEX WITH
REMARK 900  TRICHLOROMETHIAZIDEAS SULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 1CAY   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH ACETATE
REMARK 900 RELATED ID: 1CNG   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE,
REMARK 900  HCA II, CA2) MUTANT WITH GLU 117 REPLACED
REMARK 900   BY ALA (E117A)
REMARK 900 RELATED ID: 1MOO   RELATED DB: PDB
REMARK 900  SITE SPECIFIC MUTANT (H64A) OF HUMAN
REMARK 900  CARBONIC ANHYDRASE IIAT HIGH RESOLUTION
REMARK 900 RELATED ID: 2EZ7   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE ACTIVATORS. ACTIVATION OF
REMARK 900  ISOZYMES I, II,IV, VA, VII AND XIV WITH
REMARK 900   L- AND D-HISTIDINE ANDCRYSTALLOGRAPHIC
REMARK 900  ANALYSIS OF THEIR ADDUCTS WITH ISOFORMII:
REMARK 900  ENGINEERING PROTON TRANSFER PROCESSES WITHIN
REMARK 900  THEACTIVE SITE OF AN ENZYME
REMARK 900 RELATED ID: 1HEC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) MUTANT WITH LEU 198 REPLACED BY
REMARK 900  HIS (L198H)
REMARK 900 RELATED ID: 9CA2   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) MUTANT WITH VAL 143 REPLACED WITH
REMARK 900   TYR (V143Y)
REMARK 900 RELATED ID: 8CA2   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) MUTANT WITH VAL 143 REPLACED WITH
REMARK 900   HIS (V143H)
REMARK 900 RELATED ID: 1FR7   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93S
REMARK 900  /F95L/W97MCARBONIC ANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 1ZH9   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II IN COMPLEX WITH N-4
REMARK 900  -METHYL-1-PIPERAZINYL-N'-(P-SULFONAMIDE)
REMARK 900  PHENYLTHIOUREA ASSULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 1YDD   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE)(
REMARK 900  HCA II) MUTANT WITH LEU 198 REPLACED BY
REMARK 900  ARG (L198R) COMPLEXED WITH TRANSITION STATE
REMARK 900  ANALOG ACETAZOLAMIDE
REMARK 900 RELATED ID: 1BIC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH THR 200
REMARK 900  REPLACED BY HIS (T200H) COMPLEX WITH
REMARK 900  BICARBONATE
REMARK 900 RELATED ID: 1LUG   RELATED DB: PDB
REMARK 900  FULL MATRIX ERROR ANALYSIS OF CARBONIC
REMARK 900  ANHYDRASE
REMARK 900 RELATED ID: 1CAZ   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH GLU 106
REMARK 900  REPLACED BY GLN (E106Q) COMPLEX WITH ACETATE
REMARK 900 RELATED ID: 7CA2   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) MUTANT WITH VAL 143 REPLACED WITH
REMARK 900   GLY (V143G)
REMARK 900 RELATED ID: 1CVD   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) MUTANT WITH HIS 119 REPLACED BY
REMARK 900  CYS (H119C)
REMARK 900 RELATED ID: 1FR4   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND
REMARK 900  F93I/F95M/W97VCARBONIC ANHYDRASE (CAII)
REMARK 900  VARIANT
REMARK 900 RELATED ID: 4CA2   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II)
REMARK 900 RELATED ID: 2GEH   RELATED DB: PDB
REMARK 900  N-HYDROXYUREA, A VERSATILE ZINC BINDING
REMARK 900  FUNCTION IN THEDESIGN OF METALLOENZYME
REMARK 900  INHIBITORS
REMARK 900 RELATED ID: 1CIL   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH THE
REMARK 900  INHIBITOR ETS
REMARK 900 RELATED ID: 1G45   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH
REMARK 900  4-(AMINOSULFONYL)-N-[(2-FLUOROPHENYL)METHYL]-
REMARK 900  BENZAMIDE
REMARK 900 RELATED ID: 1YDB   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE)(
REMARK 900  HCA II) MUTANT WITH LEU 198 REPLACED BY
REMARK 900  PHE (L198F) COMPLEXED WITH TRANSITION STATE
REMARK 900  ANALOG ACETAZOLAMIDE
REMARK 900 RELATED ID: 2CBB   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (80 MM SODIUM CITRATE
REMARK 900  , 2.4 M AMMONIUM SULFATE, PH 6.0)
REMARK 900 RELATED ID: 1FSR   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND
REMARK 900  F93S/F95L/W97MCARBONIC ANHYDRASE (CAII)
REMARK 900  VARIANT
REMARK 900 RELATED ID: 1DCA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) MUTANT WITH THR 199 REPLACED BY
REMARK 900  CYS (T199C)
REMARK 900 RELATED ID: 1AVN   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH
REMARK 900  THE HISTAMINE ACTIVATOR
REMARK 900 RELATED ID: 12CA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) MUTANT WITH VAL 121 REPLACED BY
REMARK 900  ALA (V121A)
REMARK 900 RELATED ID: 1I9P   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH
REMARK 900  4-(AMINOSULFONYL)-N-[(2,4,6-TRIFLUOROPHENYL
REMARK 900  )METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1BCD   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH
REMARK 900  TRIFLUOROMETHANE SULPHONAMIDE
REMARK 900 RELATED ID: 1AM6   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR:
REMARK 900  ACETOHYDROXAMATE
REMARK 900 RELATED ID: 1I91   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH AL-6619
REMARK 900   2H-THIENO[3,2-E]-1,2-THIAZINE-6-
REMARK 900  SULFONAMIDE, 2-(3-HYDROXYPHENYL)-3-(4-
REMARK 900  MORPHOLINYL)-, 1,1-DIOXIDE
REMARK 900 RELATED ID: 1CVE   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE)(
REMARK 900  HCA II) MUTANT WITH HIS 119 REPLACED BY
REMARK 900  ASP (H119D)
REMARK 900 RELATED ID: 1G3Z   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V)
REMARK 900 RELATED ID: 1HEB   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) MUTANT WITH LEU 198 REPLACED BY
REMARK 900  GLU (L198E)
REMARK 900 RELATED ID: 2CBD   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (2.4 M AMMONIUM
REMARK 900  SULFATE, 0.3 M SODIUM BISULFITE, PH 7.3
REMARK 900  )
REMARK 900 RELATED ID: 1ZSC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT E117Q, HOLO
REMARK 900  FORM
REMARK 900 RELATED ID: 3CA2   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) COMPLEX WITH 3-MERCURI-4-
REMARK 900  AMINOBENZENESULFONAMIDE (AMS).
REMARK 900 RELATED ID: 1BNU   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1ZGE   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II IN COMPLEX WITH P-
REMARK 900  SULFONAMIDO-O,O'-DICHLOROANILINE AS
REMARK 900  SULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 1BNW   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 2FOV   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH
REMARK 900  TWO-PRONGINHIBITORS
REMARK 900 RELATED ID: 1TE3   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH
REMARK 900  ENVIRONMENT ON H+TRANSFER IN HUMAN CARBONIC
REMARK 900   ANHYDRASE II
REMARK 900 RELATED ID: 1BNT   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1IF5   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH 2,6-
REMARK 900  DIFLUOROBENZENESULFONAMIDE
REMARK 900 RELATED ID: 1YO1   RELATED DB: PDB
REMARK 900  PROTON TRANSFER FROM HIS200 IN HUMAN
REMARK 900  CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1G54   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH 4-(
REMARK 900  AMINOSULFONYL)-N-[(2,3,4,5,6-
REMARK 900  PENTAFLUOROPHENYL)METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1RZD   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II WITH ZINC REPLACED BY
REMARK 900   MANGANESE(II)
REMARK 900 RELATED ID: 1UGE   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II [HCAII] MUTANT
REMARK 900  WITH ALA 65 REPLACED BY LEU (A65L)
REMARK 900 RELATED ID: 2FMG   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE ACTIVATORS. ACTIVATION OF
REMARK 900  ISOFORMS I, II,IV, VA, VII AND XIV WITH
REMARK 900   L- AND D- PHENYLALANINE ANDCRYSTALLOGRAPHIC
REMARK 900  ANALYSIS OF THEIR ADDUCTS WITH ISOZYMEII:
REMARK 900  STEROSPECIFIC RECOGNITION WITHIN THE ACTIVE
REMARK 900  SITE OF ANENZYME AND ITS CONSEQUENCES FOR
REMARK 900  THE DRUG DESIGN, STRUCTUREWITH L-PHENYLALANINE
REMARK 900 RELATED ID: 1G0E   RELATED DB: PDB
REMARK 900  SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH
REMARK 900  ALA) OF HUMANCARBONIC ANHYDRASE II COMPLEXED
REMARK 900  WITH 4-METHYLIMIDAZOLE
REMARK 900 RELATED ID: 1RAY   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH AZIDE
REMARK 900 RELATED ID: 1CVA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (HCA II) MUTANT WITH
REMARK 900  THR 199 REPLACED BY VAL (T199V) (AZIDE-
REMARK 900  BOUND FORM)
REMARK 900 RELATED ID: 1CA3   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (
REMARK 900  HCA II) (PH 5.7)
REMARK 900 RELATED ID: 2EU2   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH
REMARK 900   NOVEL INHIBITORS
REMARK 900 RELATED ID: 1TG9   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH
REMARK 900  ENVIRONMENT ON H+TRANSFER IN HUMAN CARBONIC
REMARK 900   ANHYDRASE II
REMARK 900 RELATED ID: 1TBT   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH
REMARK 900  ENVIRONMENT ON H+TRANSFER IN HUMAN CARBONIC
REMARK 900   ANHYDRASE II
REMARK 900 RELATED ID: 1XEG   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE
REMARK 900   II COMPLEXEDWITH AN ACETATE ION
REMARK 900 RELATED ID: 1BN3   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1CNY   RELATED DB: PDB
REMARK 900  MOL_ID: 1; MOLECULE: CARBONIC ANHYDRASE II;
REMARK 900  CHAIN: NULL; SYNONYM: CARBONATE DEHYDRATASE,
REMARK 900  HCA II; EC: 4.2.1.1; HETEROGEN:
REMARK 900  AMINOCARBONYLBENZENESULFONAMIDE
REMARK 900 RELATED ID: 1OKM   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKM
REMARK 900   INHIBITOR 4-SULFONAMIDE-[1-(4-AMINOBUTANE)]
REMARK 900  BENZAMIDE
REMARK 900 RELATED ID: 1CNJ   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE,
REMARK 900  HCA II, CA2) MUTANT WITH GLN 92 REPLACED
REMARK 900  BY ASN (Q92N)
REMARK 900 RELATED ID: 1H9N   RELATED DB: PDB
REMARK 900  H119N CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2AW1   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE INHIBITORS: VALDECOXIB BINDS
REMARK 900   TO ADIFFERENT ACTIVE SITE REGION OF THE
REMARK 900  HUMAN ISOFORM II ASCOMPARED TO THE
REMARK 900  STRUCTURALLY RELATED CYCLOOXYGENASE II"SELECTIVE
REMARK 900  " INHIBITOR CELECOXIB
REMARK 900 RELATED ID: 1H4N   RELATED DB: PDB
REMARK 900  H94N CARBONIC ANHYDRASE II COMPLEXED WITH
REMARK 900  TRIS
REMARK 900 RELATED ID: 2FOS   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH
REMARK 900  TWO-PRONGINHIBITORS
REMARK 900 RELATED ID: 1H9Q   RELATED DB: PDB
REMARK 900  H119Q CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2VVB   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH
REMARK 900   BICARBONATE
DBREF  2VVA X    1   125  UNP    P00918   CAH2_HUMAN       1    125
DBREF  2VVA X  127   261  UNP    P00918   CAH2_HUMAN     126    260
SEQRES   1 X  260  MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES   2 X  260  GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES   3 X  260  ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES   4 X  260  TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES   5 X  260  GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES   6 X  260  PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES   7 X  260  LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES   8 X  260  GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES   9 X  260  SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES  10 X  260  LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES  11 X  260  GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 X  260  GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES  13 X  260  GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES  14 X  260  GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES  15 X  260  LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES  16 X  260  SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES  17 X  260  ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES  18 X  260  VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES  19 X  260  GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES  20 X  260  GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET    SO4  X1262       5
HET    CO2  X1263       3
HET    CO2  X1264       3
HET    GOL  X1265       6
HET    GOL  X1266       6
HET     ZN  X1267       1
HETNAM     CO2 CARBON DIOXIDE
HETNAM     SO4 SULFATE ION
HETNAM     GOL GLYCEROL
HETNAM      ZN ZINC ION
FORMUL   2  CO2    2(C O2)
FORMUL   3  SO4    O4 S 2-
FORMUL   4  GOL    2(C3 H8 O3)
FORMUL   5   ZN    ZN 2+
FORMUL   6  HOH   *350(H2 O1)
HELIX    1   1 GLY X   12  TRP X   16  5                                   5
HELIX    2   2 PHE X   20  GLY X   25  5                                   6
HELIX    3   3 LYS X  127  GLY X  129  5                                   3
HELIX    4   4 ASP X  130  VAL X  135  1                                   6
HELIX    5   5 LYS X  154  GLY X  156  5                                   3
HELIX    6   6 LEU X  157  LEU X  164  1                                   8
HELIX    7   7 ASP X  165  LYS X  168  5                                   4
HELIX    8   8 ASP X  180  LEU X  185  5                                   6
HELIX    9   9 SER X  219  ARG X  227  1                                   9
SHEET    1  XA 2 ASP X  32  ILE X  33  0
SHEET    2  XA 2 THR X 108  VAL X 109  1  O  THR X 108   N  ILE X  33
SHEET    1  XB 7 LYS X  39  TYR X  40  0
SHEET    2  XB 7 LYS X 257  ALA X 258  1  N  ALA X 258   O  LYS X  39
SHEET    3  XB 7 TYR X 191  GLY X 196 -1  O  THR X 193   N  LYS X 257
SHEET    4  XB 7 VAL X 207  LEU X 212 -1  O  VAL X 207   N  GLY X 196
SHEET    5  XB 7 LEU X 141  VAL X 150  1  O  LEU X 141   N  THR X 208
SHEET    6  XB 7 ALA X 116  ASN X 124 -1  O  ALA X 116   N  LEU X 148
SHEET    7  XB 7 TYR X  88  TRP X  97 -1  O  ARG X  89   N  TRP X 123
SHEET    1  XC 6 LYS X  39  TYR X  40  0
SHEET    2  XC 6 LYS X 257  ALA X 258  1  N  ALA X 258   O  LYS X  39
SHEET    3  XC 6 TYR X 191  GLY X 196 -1  O  THR X 193   N  LYS X 257
SHEET    4  XC 6 VAL X 207  LEU X 212 -1  O  VAL X 207   N  GLY X 196
SHEET    5  XC 6 LEU X 141  VAL X 150  1  O  LEU X 141   N  THR X 208
SHEET    6  XC 6 ILE X 216  VAL X 218  1  O  ILE X 216   N  LYS X 149
LINK        ZN    ZN X1267                 NE2 HIS X  96     1555   1555  2.03
LINK        ZN    ZN X1267                 ND1 HIS X 119     1555   1555  2.01
LINK        ZN    ZN X1267                 NE2 HIS X  94     1555   1555  2.04
LINK        ZN    ZN X1267                 O   HOH X2350     1555   1555  1.97
CISPEP   1 SER X   29    PRO X   30          0        -0.03
CISPEP   2 PRO X  201    PRO X  202          0        11.92
SITE     1 AC1  8 HIS X  64  ASN X  67  HOH X2158  HOH X2339
SITE     2 AC1  8 HOH X2341  HOH X2342  HOH X2343  HOH X2344
SITE     1 AC2  6 PHE X  95  TRP X  97  ALA X 116  LEU X 148
SITE     2 AC2  6 VAL X 223  PHE X 226
SITE     1 AC3  8 HIS X  94  HIS X 119  VAL X 121  LEU X 198
SITE     2 AC3  8 THR X 199  TRP X 209   ZN X1267  HOH X2350
SITE     1 AC4  5 TYR X 114  LYS X 149  PRO X 215  HOH X2346
SITE     2 AC4  5 HOH X2347
SITE     1 AC5  8 HIS X  17  LYS X  24  SER X 188  LEU X 189
SITE     2 AC5  8 ASP X 190  HOH X2035  HOH X2348  HOH X2349
SITE     1 AC6  5 HIS X  94  HIS X  96  HIS X 119  CO2 X1264
SITE     2 AC6  5 HOH X2350
CRYST1   42.589   41.577   72.636  90.00 104.84  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      0.023480  0.000000  0.006221        0.00000
SCALE2      0.000000  0.024052  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014242        0.00000
      
PROCHECK
Go to PROCHECK summary
 References