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PDBsum entry 2weh

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Lyase PDB id
2weh
Jmol
Contents
Protein chain
258 a.a.
Ligands
FB1
GOL
Metals
_ZN
Waters ×137
HEADER    LYASE                                   31-MAR-09   2WEH
TITLE     THERMODYNAMIC OPTIMISATION OF CARBONIC ANHYDRASE FRAGMENT
TITLE    2 INHIBITORS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 2-260;
COMPND   5 SYNONYM: CARBONIC ANHYDRASE II, CARBONATE DEHYDRATASE II,
COMPND   6  CARBONIC ANHYDRASE C, CA-II, CAC;
COMPND   7 EC: 4.2.1.1;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    METAL-BINDING, DISEASE MUTATION, LYASE, ZINC, CYTOPLASM,
KEYWDS   2 ACETYLATION, POLYMORPHISM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.D.SCOTT,C.PHILLIPS,A.ALEX,A.BENT,R.O'BRIEN,L.DAMIAN,
AUTHOR   2 L.H.JONES
REVDAT   2   15-JUN-11 2WEH    1       JRNL   REMARK HETNAM HETSYN
REVDAT   2 2                           FORMUL
REVDAT   1   10-NOV-09 2WEH    0
JRNL        AUTH   A.D.SCOTT,C.PHILLIPS,A.ALEX,M.FLOCCO,A.BENT,
JRNL        AUTH 2 A.RANDALL,R.O'BRIEN,L.DAMIAN,L.H.JONES
JRNL        TITL   THERMODYNAMIC OPTIMISATION IN DRUG DISCOVERY: A
JRNL        TITL 2 CASE STUDY USING CARBONIC ANHYDRASE INHIBITORS.
JRNL        REF    CHEMMEDCHEM                   V.   4  1985 2009
JRNL        REFN                   ISSN 1860-7179
JRNL        PMID   19882701
JRNL        DOI    10.1002/CMDC.200900386
REMARK   2
REMARK   2 RESOLUTION.    2.10 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) : 2.09
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.31
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 13715
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) : 0.169
REMARK   3   R VALUE            (WORKING SET) : 0.165
REMARK   3   FREE R VALUE                     : 0.241
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 724
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) : 2.09
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 992
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.21
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1680
REMARK   3   BIN FREE R VALUE SET COUNT          : 49
REMARK   3   BIN FREE R VALUE                    : 0.2940
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2058
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 18
REMARK   3   SOLVENT ATOMS            : 137
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.18
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.01000
REMARK   3    B33 (A**2) : 0.00000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.01000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.237
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.207
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.137
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.033
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.892
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2135 ; 0.027 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2895 ; 2.140 ; 1.954
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   256 ; 7.252 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    99 ;35.622 ;24.646
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   353 ;16.166 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;24.165 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   301 ; 0.152 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1637 ; 0.011 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1013 ; 0.240 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1391 ; 0.321 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   163 ; 0.166 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     4 ; 0.100 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    33 ; 0.218 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.136 ; 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):  1336 ; 1.470 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2071 ; 2.178 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   956 ; 3.598 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   824 ; 4.850 ; 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 : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2WEH COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  01-APR-09.
REMARK 100 THE PDBE ID CODE IS EBI-39285.
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        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14449
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 3.1
REMARK 200  R MERGE                    (I) : 0.18
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 37.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       20.61150
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 DETERMNED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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    GLU A 117   CB    GLU A 117   CG      0.117
REMARK 500    THR A 125   C     LYS A 127   N       0.209
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    LEU A  47   CB  -  CG  -  CD1 ANGL. DEV. = -10.9 DEGREES
REMARK 500    LEU A  60   CB  -  CG  -  CD1 ANGL. DEV. =  10.6 DEGREES
REMARK 500    LEU A  60   CB  -  CG  -  CD2 ANGL. DEV. = -10.9 DEGREES
REMARK 500    ASP A 130   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 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    ARG A  27       56.01   -142.49
REMARK 500    LYS A 111       -6.61     77.92
REMARK 500    PHE A 176       66.11   -152.84
REMARK 500    ASN A 244       58.63    -91.97
REMARK 500    LYS A 252     -124.80     46.65
REMARK 500    ASN A 253       57.93    -95.99
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 A1262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  96   NE2
REMARK 620 2 HIS A 119   ND1  98.1
REMARK 620 3 HIS A  94   NE2 109.3 117.0
REMARK 620 4 FB1 A1263   N   111.9 113.2 107.2
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  ZN A1262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FB1 A1263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1264
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OKL   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKL INHIBITOR 5-
REMARK 900 DIMETHYLAMINO-NAPHTHALENE-1- SULFONAMIDE
REMARK 900 RELATED ID: 1I9Q   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-
REMARK 900 (AMINOSULFONYL)-N-[(3,4,5-TRIFLUOROPHENYL )METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1ZFQ   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II IN COMPLEX WITH ETHOXZOLAMIDPHENOLEAS
REMARK 900 SULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 1IF7   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH (R)-N -(3-INDOL-1-YL-2-
REMARK 900 METHYL-PROPYL)-4- SULFAMOYL-BENZAMIDE
REMARK 900 RELATED ID: 1CAM   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT WITH THR 199 REPLACED BY ALA
REMARK 900 (T199A) COMPLEX WITH BICARBONATE
REMARK 900 RELATED ID: 1T9N   RELATED DB: PDB
REMARK 900 EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+TRANSFER
REMARK 900 IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1CNW   RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: CARBONIC ANHYDRASE II; CHAIN: NULL;
REMARK 900 SYNONYM: CARBONATE DEHYDRATASE, HCA II; EC: 4.2.1.1;
REMARK 900 HETEROGEN: ETHYLAMINOCARBONYLBENZENESULFONAMIDE
REMARK 900 RELATED ID: 1OKN   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKN INHIBITOR 4-
REMARK 900 SULFONAMIDE-[1-(4-N-(5- FLUORESCEIN THIOUREA)BUTANE)]
REMARK 900 RELATED ID: 1F2W   RELATED DB: PDB
REMARK 900 THE MECHANISM OF CYANAMIDE HYDRATION CATALYZED BY CARBONIC
REMARK 900 ANHYDRASE II REVEALED BY CRYOGENIC X-RAY DIFFRACTION
REMARK 900 RELATED ID: 1G52   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH 4-( AMINOSULFONYL)-N-
REMARK 900 [(2,3-DIFLUOROPHENYL)METHYL ]-BENZAMIDE
REMARK 900 RELATED ID: 2H4N   RELATED DB: PDB
REMARK 900 H94N CARBONIC ANHYDRASE II COMPLEXED WITH ACETAZOLAMIDE
REMARK 900 RELATED ID: 1BNM   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1CNH   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II, CA2)
REMARK 900 MUTANT WITH GLN 92 REPLACED BY GLU (Q92E)
REMARK 900 RELATED ID: 1BNQ   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1UGC   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II [HCAII] MUTANT WITH ALA 65
REMARK 900 REPLACED BY HIS (A65H)
REMARK 900 RELATED ID: 1XEV   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN A
REMARK 900 NEWCRYSTAL FORM
REMARK 900 RELATED ID: 1IF9   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH N-[2-( 1H-INDOL-5-YL)-
REMARK 900 BUTYL]-4-SULFAMOYL- BENZAMIDE
REMARK 900 RELATED ID: 1UGG   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II[HCAII] MUTANT WITH ALA 65
REMARK 900 REPLACED BY SER (A65S) - ORTHORHOMBIC FORM
REMARK 900 RELATED ID: 1G53   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH 4-( AMINOSULFONYL)-N-
REMARK 900 [(2,6-DIFLUOROPHENYL)METHYL ]-BENZAMIDE
REMARK 900 RELATED ID: 1FQM   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93I /F95M/
REMARK 900 W97VCARBONIC ANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 1CA2   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
REMARK 900 RELATED ID: 1FQL   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F95M /W97V
REMARK 900 CARBONICANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 1CAL   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT WITH THR 199 REPLACED BY ALA
REMARK 900 (T199A)
REMARK 900 RELATED ID: 1I9N   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-
REMARK 900 (AMINOSULFONYL)-N-[(2,5-DIFLUOROPHENYL) METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1G4O   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-
REMARK 900 (AMINOSULFONYL)-N-PHENYLMETHYLBENZAMIDE
REMARK 900 RELATED ID: 2CBA   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (50 MM TRIS, 3 M AMMONIUM SULFATE, PH
REMARK 900 7.8)
REMARK 900 RELATED ID: 1YDC   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
REMARK 900 MUTANT WITH LEU 198 REPLACED BY PHE (L198F)
REMARK 900 RELATED ID: 1CCS   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II)
REMARK 900 MUTANT WITH THR 199 REPLACED BY ASP (T199D)
REMARK 900 RELATED ID: 1LZV   RELATED DB: PDB
REMARK 900 SITE-SPECIFIC MUTANT (TYR7 REPLACED WITH HIS ) OF
REMARK 900 HUMANCARBONIC ANHYDRASE II
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 F93I/F95M/
REMARK 900 W97VCARBONIC ANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 1A42   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH BRINZOLAMIDE
REMARK 900 RELATED ID: 1RZB   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II WITH ZINC REPLACED BY BY COBALT(II)
REMARK 900 AT PH 6.0
REMARK 900 RELATED ID: 1TH9   RELATED DB: PDB
REMARK 900 EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+TRANSFER
REMARK 900 IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1ZSB   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT E117Q, TRANSITION STATE
REMARK 900 ANALOGUE ACETAZOLAMIDE
REMARK 900 RELATED ID: 1CNB   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II)
REMARK 900 MUTANT WITH HIS 94 REPLACED BY CYS (H94C) COMPLEXED WITH
REMARK 900 BETA-MERCAPTOETHANOL (BME)
REMARK 900 RELATED ID: 1HED   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
REMARK 900 MUTANT WITH LEU 198 REPLACED BY ALA (L198A)
REMARK 900 RELATED ID: 1I8Z   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH AL-6629 2H-THIENO[3,2-
REMARK 900 E]-1,2-THIAZINE-6- SULFONAMIDE, 2-(3-METHOXYPHENYL)-3-(4-
REMARK 900 MORPHOLINYL)-, 1,1-DIOXIDE
REMARK 900 RELATED ID: 1G48   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-
REMARK 900 (AMINOSULFONYL)-N-[(2,6-DIFLUOROPHENYL) METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1LG5   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE HCA II MUTANT T199P
REMARK 900 INCOMPLEX WITH BETA- MERCAPTOETHANOL
REMARK 900 RELATED ID: 1BV3   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH UREA
REMARK 900 RELATED ID: 1G0F   RELATED DB: PDB
REMARK 900 SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH ALA) OF
REMARK 900 HUMANCARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1TG3   RELATED DB: PDB
REMARK 900 EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+TRANSFER
REMARK 900 IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1CVC   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT WITH HIS 94 REPLACED BY ASP
REMARK 900 (H94D)
REMARK 900 RELATED ID: 1UGD   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II[HCAII] MUTANT WITH ALA 65
REMARK 900 REPLACED BY SER (A65S)
REMARK 900 RELATED ID: 1YO0   RELATED DB: PDB
REMARK 900 PROTON TRANSFER FROM HIS200 IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1I90   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH AL-8520 2H-THIENO[3,2-
REMARK 900 E]-1,2-THIAZINE-6- SULFONAMIDE, 4-AMINO-3,4-DIHYDRO-2-(3-
REMARK 900 METHOXYPROPYL)-, 1,1-DIOXIDE, (R)
REMARK 900 RELATED ID: 2WD3   RELATED DB: PDB
REMARK 900 FIRST DUAL AROMATASE-STEROID SULFATASE INHIBITORS BASED ON
REMARK 900 A BIPHENYL TEMPLATE
REMARK 900 RELATED ID: 1HVA   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT WITH HIS 94 REPLACED BY CYS
REMARK 900 (H94C)
REMARK 900 RELATED ID: 1FSN   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF METAL-FREE F93S /F95L/
REMARK 900 W97MCARBONIC ANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 1RZE   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II WITH ZINC REPLACED BY NICKEL(II)
REMARK 900 RELATED ID: 1UGB   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II[HCAII] MUTANT WITH ALA 65
REMARK 900 REPLACED BY GLY (A65G)
REMARK 900 RELATED ID: 1Z9Y   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II IN COMPLEX WITH FUROSEMIDE
REMARK 900 ASSULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 2FMZ   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE ACTIVATORS. ACTIVATION OF ISOFORMS I, II,
REMARK 900 IV, VA, VII AND XIV WITH L- AND D- PHENYLALANINE,STRUCTURE
REMARK 900 WITH D- PHENYLALANINE.
REMARK 900 RELATED ID: 1CNK   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II, CA2)
REMARK 900 MUTANT WITH GLN 92 REPLACED 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 ENVIRONMENT ON H+TRANSFER
REMARK 900 IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1RZA   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II WITH ZINC REPLACED BY COBALT(II)
REMARK 900 RELATED ID: 2VVB   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH BICARBONATE
REMARK 900 RELATED ID: 1CCU   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II)
REMARK 900 MUTANT WITH THR 199 REPLACED BY HIS (T199H)
REMARK 900 RELATED ID: 1I9L   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-
REMARK 900 (AMINOSULFONYL)-N-[(4-FLUOROPHENYL)METHYL]- BENZAMIDE
REMARK 900 RELATED ID: 2CBC   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (50 MM TRIS, 3 M AMMONIUM SULFATE,
REMARK 900 0.2 FORMATE, PH 7.6)
REMARK 900 RELATED ID: 1G46   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-
REMARK 900 (AMINOSULFONYL)-N-[(2,3-DIFLUOROPHENYL) METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1CVB   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (HCA II) MUTANT WITH THR 199 REPLACED
REMARK 900 BY VAL (T199V) (SULFATE- BOUND FORM)
REMARK 900 RELATED ID: 1CAO   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEX WITH HYDROGEN SULFIDE
REMARK 900 RELATED ID: 1FSQ   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND F93S/F95L/
REMARK 900 W97MCARBONIC ANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 6CA2   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
REMARK 900 MUTANT WITH VAL 143 REPLACED WITH PHE (V143F)
REMARK 900 RELATED ID: 5CA2   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
REMARK 900 (MUTANT WITH THR 200 REPLACED WITH SER) (T200S)
REMARK 900 RELATED ID: 1G1D   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH 4-( AMINOSULFONYL)-N-
REMARK 900 [(2-FLUOROPHENYL)METHYL]- BENZAMIDE
REMARK 900 RELATED ID: 1CAJ   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT WITH GLU 106 REPLACED BY ASP
REMARK 900 (E106D)
REMARK 900 RELATED ID: 1CVF   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
REMARK 900 MUTANT WITH HIS 94 REPLACED BY ALA (H94A)
REMARK 900 RELATED ID: 2FOU   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH TWO-
REMARK 900 PRONGINHIBITORS
REMARK 900 RELATED ID: 1LGD   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF HCA II MUTANT T199P INCOMPLEX
REMARK 900 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 ENVIRONMENT ON H+TRANSFER
REMARK 900 IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1CRA   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEX WITH 1,2,4- TRIAZOLE
REMARK 900 RELATED ID: 1IF4   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH 4-
REMARK 900 FLUOROBENZENESULFONAMIDE
REMARK 900 RELATED ID: 1ZE8   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II IN COMPLEX WITH A MEMBRANE-
REMARK 900 IMPERMEANTSULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 1HEA   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
REMARK 900 MUTANT WITH LEU 198 REPLACED BY ARG (L198R)
REMARK 900 RELATED ID: 1CAH   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (NATIVE ZINC REPLACED BY COBALT)
REMARK 900 COMPLEX WITH BICARBONATE
REMARK 900 RELATED ID: 1HCA   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II) (PH
REMARK 900 6.5)
REMARK 900 RELATED ID: 1G4J   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-
REMARK 900 (AMINOSULFONYL)-N-[(2,3,4,5,6- PENTAFLUOROPHENYL)METHYL]-
REMARK 900 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 INHIBITOR 2000-07
REMARK 900 RELATED ID: 1CIM   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH THE INHIBITOR PTS
REMARK 900 RELATED ID: 1CVH   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE II, HCA II)
REMARK 900 MUTANT WITH HIS 96 REPLACED BY CYS (H96C)
REMARK 900 RELATED ID: 1CIN   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH THE INHIBITOR MTS
REMARK 900 RELATED ID: 1IF8   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH (S)-N -(3-INDOL-1-YL-2-
REMARK 900 METHYL-PROPYL)-4- SULFAMOYL-BENZAMIDE
REMARK 900 RELATED ID: 1I9M   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-
REMARK 900 (AMINOSULFONYL)-N-[(2,4-DIFLUOROPHENYL) METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1ZFK   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II IN COMPLEX WITH N-4 -SULFONAMIDPHENYL-
REMARK 900 N'-4-METHYLBENZOSULFONYLUREASE AS SULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 1FQN   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF METAL-FREE F93I /F95M/
REMARK 900 W97VCARBONIC ANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 1ZSA   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT E117Q, APO FORM
REMARK 900 RELATED ID: 1LG6   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF HCA II MUTANT T199P INCOMPLEX
REMARK 900 WITH THIOCYANATE
REMARK 900 RELATED ID: 1CNC   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II)
REMARK 900 MUTANT WITH HIS 94 REPLACED BY CYS (H94C) COMPLEXED WITH
REMARK 900 ZINC
REMARK 900 RELATED ID: 1UGA   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II[HCAII] MUTANT WITH ALA 65
REMARK 900 REPLACED BY PHE (A65F)
REMARK 900 RELATED ID: 1BNN   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1TB0   RELATED DB: PDB
REMARK 900 EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+TRANSFER
REMARK 900 IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2FOQ   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH TWO-
REMARK 900 PRONGINHIBITORS
REMARK 900 RELATED ID: 1CAI   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT WITH GLU 106 REPLACED BY ALA
REMARK 900 (E106A)
REMARK 900 RELATED ID: 2AX2   RELATED DB: PDB
REMARK 900 PRODUCTION AND X-RAY CRYSTALLOGRAPHIC ANALYSIS OF
REMARK 900 FULLYDEUTERATED HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1DCB   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
REMARK 900 MUTANT WITH THR 199 REPLACED BY CYS (T199C)
REMARK 900 RELATED ID: 1CNX   RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: CARBONIC ANHYDRASE II; CHAIN: NULL;
REMARK 900 SYNONYM: CARBONATE DEHYDRATASE, HCA II; EC: 4.2.1.1;
REMARK 900 HETEROGEN: BENZENESULFONAMIDE
REMARK 900 RELATED ID: 2HD6   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CARBONIC ANHYDRASE II
REMARK 900 INCOMPLEX WITH A HYPOXIA- ACTIVATABLE SULFONAMIDE.
REMARK 900 RELATED ID: 5CAC   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE FORM C COMPLEX WITH HYDROGEN SULFITE
REMARK 900 RELATED ID: 4CAC   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE FORM C (PH 6)
REMARK 900 RELATED ID: 1TTM   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH 667-COUMATE
REMARK 900 RELATED ID: 1CAK   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT WITH GLU 106 REPLACED BY GLN
REMARK 900 (E106Q)
REMARK 900 RELATED ID: 1I9O   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-
REMARK 900 (AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL) METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1CNI   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II, CA2)
REMARK 900 MUTANT WITH GLN 92 REPLACED BY ALA (Q92A)
REMARK 900 RELATED ID: 1CAN   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEX WITH NITRATE
REMARK 900 RELATED ID: 1YDA   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
REMARK 900 MUTANT WITH LEU 198 REPLACED BY GLU (L198E) COMPLEXED WITH
REMARK 900 TRANSITION STATE ANALOG ACETAZOLAMIDE
REMARK 900 RELATED ID: 2EU3   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH NOVEL INHIBITORS
REMARK 900 RELATED ID: 2WD2   RELATED DB: PDB
REMARK 900 A CHIMERIC MICROTUBULE DISRUPTOR WITH EFFICACY ON A TAXANE
REMARK 900 RESISTANT CELL LINE
REMARK 900 RELATED ID: 1EOU   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II
REMARK 900 COMPLEXEDWITH AN ANTICONVULSANT SUGAR SULFAMATE
REMARK 900 RELATED ID: 1YO2   RELATED DB: PDB
REMARK 900 PROTON TRANSFER FROM HIS200 IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1MUA   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT WITH PRO 202 REPLACED BY ALA
REMARK 900 (P202A)
REMARK 900 RELATED ID: 2CA2   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) ( HCA II)
REMARK 900 COMPLEX WITH THIOCYANATE ION
REMARK 900 RELATED ID: 1CCT   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II)
REMARK 900 MUTANT WITH THR 199 REPLACED BY GLU (T199E)
REMARK 900 RELATED ID: 2ABE   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE ACTIVATORS: X-RAY CRYSTAL STRUCTURE
REMARK 900 OFTHE ADDUCT OF HUMAN ISOZYME II WITH L-HISTIDINE AS
REMARK 900 APLATFORM FOR THE DESIGN OF STRONGER ACTIVATORS
REMARK 900 RELATED ID: 1OQ5   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II IN COMPLEX WITH NANOMOLAR INHIBITOR
REMARK 900 RELATED ID: 1RZC   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II WITH ZINC REPLACED BY COPPER(II)
REMARK 900 RELATED ID: 1UGF   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II [HCAII] MUTANT WITH ALA 65
REMARK 900 REPLACED BY THR (A65T)
REMARK 900 RELATED ID: 1THK   RELATED DB: PDB
REMARK 900 EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+TRANSFER
REMARK 900 IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2CBE   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (50 MM TRIS, 3 M AMMONIUM SULFATE,
REMARK 900 2MM DIPICOLINATE, PH 7.8)
REMARK 900 RELATED ID: 1KWR   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH INHIBITOR 0134-36
REMARK 900 RELATED ID: 1ZGF   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II IN COMPLEX WITH TRICHLOROMETHIAZIDEAS
REMARK 900 SULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 1CAY   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEX WITH ACETATE
REMARK 900 RELATED ID: 1MOO   RELATED DB: PDB
REMARK 900 SITE SPECIFIC MUTANT (H64A) OF HUMAN CARBONIC ANHYDRASE
REMARK 900 IIAT HIGH RESOLUTION
REMARK 900 RELATED ID: 1CNG   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II, CA2)
REMARK 900 MUTANT WITH GLU 117 REPLACED BY ALA (E117A)
REMARK 900 RELATED ID: 2EZ7   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE ACTIVATORS. ACTIVATION OF ISOZYMES I, II,
REMARK 900 IV, VA, VII AND XIV WITH L- AND D-HISTIDINE
REMARK 900 ANDCRYSTALLOGRAPHIC ANALYSIS OF THEIR ADDUCTS WITH
REMARK 900 ISOFORMII: 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) (HCA II)
REMARK 900 MUTANT WITH LEU 198 REPLACED BY HIS (L198H)
REMARK 900 RELATED ID: 8CA2   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
REMARK 900 MUTANT WITH VAL 143 REPLACED WITH HIS (V143H)
REMARK 900 RELATED ID: 9CA2   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
REMARK 900 MUTANT WITH VAL 143 REPLACED WITH TYR (V143Y)
REMARK 900 RELATED ID: 1FR7   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93S /F95L/
REMARK 900 W97MCARBONIC ANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 1ZH9   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II IN COMPLEX WITH N-4 -METHYL-1-
REMARK 900 PIPERAZINYL-N'-(P-SULFONAMIDE) PHENYLTHIOUREA ASSULFONAMIDE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 1YDD   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE)( HCA II)
REMARK 900 MUTANT WITH LEU 198 REPLACED BY ARG (L198R) COMPLEXED WITH
REMARK 900 TRANSITION STATE ANALOG ACETAZOLAMIDE
REMARK 900 RELATED ID: 1LUG   RELATED DB: PDB
REMARK 900 FULL MATRIX ERROR ANALYSIS OF CARBONIC ANHYDRASE
REMARK 900 RELATED ID: 1BIC   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT WITH THR 200 REPLACED BY HIS
REMARK 900 (T200H) COMPLEX WITH BICARBONATE
REMARK 900 RELATED ID: 1CAZ   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT WITH GLU 106 REPLACED BY GLN
REMARK 900 (E106Q) COMPLEX WITH ACETATE
REMARK 900 RELATED ID: 7CA2   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) ( HCA II)
REMARK 900 MUTANT WITH VAL 143 REPLACED WITH GLY (V143G)
REMARK 900 RELATED ID: 1CVD   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) ( HCA II)
REMARK 900 MUTANT WITH HIS 119 REPLACED BY CYS (H119C)
REMARK 900 RELATED ID: 1FR4   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93I/F95M/
REMARK 900 W97VCARBONIC ANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 2GEH   RELATED DB: PDB
REMARK 900 N-HYDROXYUREA, A VERSATILE ZINC BINDING FUNCTION IN
REMARK 900 THEDESIGN OF METALLOENZYME INHIBITORS
REMARK 900 RELATED ID: 4CA2   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) ( HCA II)
REMARK 900 RELATED ID: 1CIL   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH THE INHIBITOR ETS
REMARK 900 RELATED ID: 1G45   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-
REMARK 900 (AMINOSULFONYL)-N-[(2-FLUOROPHENYL)METHYL]- BENZAMIDE
REMARK 900 RELATED ID: 1YDB   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE)( HCA II)
REMARK 900 MUTANT WITH LEU 198 REPLACED BY PHE (L198F) COMPLEXED WITH
REMARK 900 TRANSITION STATE ANALOG ACETAZOLAMIDE
REMARK 900 RELATED ID: 1DCA   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) ( HCA II)
REMARK 900 MUTANT WITH THR 199 REPLACED BY CYS (T199C)
REMARK 900 RELATED ID: 1FSR   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93S/F95L/
REMARK 900 W97MCARBONIC ANHYDRASE (CAII) VARIANT
REMARK 900 RELATED ID: 2CBB   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (80 MM SODIUM CITRATE , 2.4 M
REMARK 900 AMMONIUM SULFATE, PH 6.0)
REMARK 900 RELATED ID: 1AVN   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH THE HISTAMINE
REMARK 900 ACTIVATOR
REMARK 900 RELATED ID: 1I9P   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-
REMARK 900 (AMINOSULFONYL)-N-[(2,4,6-TRIFLUOROPHENYL )METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 12CA   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) ( HCA II)
REMARK 900 MUTANT WITH VAL 121 REPLACED BY ALA (V121A)
REMARK 900 RELATED ID: 1BCD   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEX WITH TRIFLUOROMETHANE
REMARK 900 SULPHONAMIDE
REMARK 900 RELATED ID: 1I91   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH AL-6619 2H-THIENO[3,2-
REMARK 900 E]-1,2-THIAZINE-6- SULFONAMIDE, 2-(3-HYDROXYPHENYL)-3-(4-
REMARK 900 MORPHOLINYL)-, 1,1-DIOXIDE
REMARK 900 RELATED ID: 1AM6   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II INHIBITOR: ACETOHYDROXAMATE
REMARK 900 RELATED ID: 1CVE   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE)( HCA II)
REMARK 900 MUTANT WITH HIS 119 REPLACED BY 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) ( HCA II)
REMARK 900 MUTANT WITH LEU 198 REPLACED BY GLU (L198E)
REMARK 900 RELATED ID: 2CBD   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (2.4 M AMMONIUM SULFATE, 0.3 M SODIUM
REMARK 900 BISULFITE, PH 7.3)
REMARK 900 RELATED ID: 1ZSC   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT E117Q, HOLO FORM
REMARK 900 RELATED ID: 1BNU   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 3CA2   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) ( HCA II)
REMARK 900 COMPLEX WITH 3-MERCURI-4- AMINOBENZENESULFONAMIDE (AMS).
REMARK 900 RELATED ID: 1BNW   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- SULFONAMIDO-O,O'-
REMARK 900 DICHLOROANILINE AS SULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 1TE3   RELATED DB: PDB
REMARK 900 EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+TRANSFER
REMARK 900 IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2FOV   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH TWO-
REMARK 900 PRONGINHIBITORS
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 CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1RZD   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II WITH ZINC REPLACED BY MANGANESE(II)
REMARK 900 RELATED ID: 1G54   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH 4-( AMINOSULFONYL)-N-
REMARK 900 [(2,3,4,5,6- PENTAFLUOROPHENYL)METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1UGE   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II [HCAII] MUTANT WITH ALA 65
REMARK 900 REPLACED BY LEU (A65L)
REMARK 900 RELATED ID: 1G0E   RELATED DB: PDB
REMARK 900 SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH ALA) OF
REMARK 900 HUMANCARBONIC ANHYDRASE II COMPLEXED WITH 4-METHYLIMIDAZOLE
REMARK 900 RELATED ID: 2FMG   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE ACTIVATORS. ACTIVATION OF ISOFORMS I, II,
REMARK 900 IV, VA, VII AND XIV WITH L- AND D- PHENYLALANINE
REMARK 900 ANDCRYSTALLOGRAPHIC ANALYSIS OF THEIR ADDUCTS WITH
REMARK 900 ISOZYMEII: STEROSPECIFIC RECOGNITION WITHIN THE ACTIVE SITE
REMARK 900 OF ANENZYME AND ITS CONSEQUENCES FOR THE DRUG DESIGN,
REMARK 900 STRUCTUREWITH L-PHENYLALANINE
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 THR 199 REPLACED
REMARK 900 BY VAL (T199V) (AZIDE- BOUND FORM)
REMARK 900 RELATED ID: 1CA3   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) ( HCA II) (PH
REMARK 900 5.7)
REMARK 900 RELATED ID: 2EU2   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH NOVEL INHIBITORS
REMARK 900 RELATED ID: 1TG9   RELATED DB: PDB
REMARK 900 EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+TRANSFER
REMARK 900 IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1TBT   RELATED DB: PDB
REMARK 900 EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+TRANSFER
REMARK 900 IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1XEG   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II
REMARK 900 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; CHAIN: NULL;
REMARK 900 SYNONYM: CARBONATE DEHYDRATASE, HCA II; EC: 4.2.1.1;
REMARK 900 HETEROGEN: AMINOCARBONYLBENZENESULFONAMIDE
REMARK 900 RELATED ID: 1OKM   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKM INHIBITOR 4-
REMARK 900 SULFONAMIDE-[1-(4-AMINOBUTANE)] BENZAMIDE
REMARK 900 RELATED ID: 1CNJ   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II, CA2)
REMARK 900 MUTANT WITH GLN 92 REPLACED BY ASN (Q92N)
REMARK 900 RELATED ID: 1H9N   RELATED DB: PDB
REMARK 900 H119N CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2VVA   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE IN COMPLEX WITH CO2
REMARK 900 RELATED ID: 2AW1   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE INHIBITORS: VALDECOXIB BINDS TO
REMARK 900 ADIFFERENT ACTIVE SITE REGION OF THE HUMAN ISOFORM II
REMARK 900 ASCOMPARED TO THE STRUCTURALLY RELATED CYCLOOXYGENASE II"
REMARK 900 SELECTIVE " INHIBITOR CELECOXIB
REMARK 900 RELATED ID: 1H4N   RELATED DB: PDB
REMARK 900 H94N CARBONIC ANHYDRASE II COMPLEXED WITH TRIS
REMARK 900 RELATED ID: 2FOS   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH TWO-
REMARK 900 PRONGINHIBITORS
REMARK 900 RELATED ID: 1H9Q   RELATED DB: PDB
REMARK 900 H119Q CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2WEG   RELATED DB: PDB
REMARK 900 THERMODYNAMIC OPTIMISATION OF CARBONIC ANHYDRASE FRAGMENT
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2WEJ   RELATED DB: PDB
REMARK 900 THERMODYNAMIC OPTIMISATION OF CARBONIC ANHYDRASE FRAGMENT
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 2WEO   RELATED DB: PDB
REMARK 900 THERMODYNAMIC OPTIMISATION OF CARBONIC ANHYDRASE FRAGMENT
REMARK 900 INHIBITORS
DBREF  2WEH A    2   261  UNP    P00918   CAH2_HUMAN       2    260
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     ZN  A1262       1
HET    FB1  A1263      11
HET    GOL  A1264       6
HETNAM      ZN ZINC ION
HETNAM     FB1 2-CHLOROBENZENESULFONAMIDE
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN
FORMUL   2   ZN    ZN 2+
FORMUL   3  FB1    C6 H6 N1 O2 CL1 S1
FORMUL   4  GOL    C3 H8 O3
FORMUL   5  HOH   *137(H2 O)
HELIX    1   1 GLY A   12  ASP A   19  5                                   8
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A  127  GLY A  129  5                                   3
HELIX    4   4 ASP A  130  VAL A  135  1                                   6
HELIX    5   5 LYS A  154  GLY A  156  5                                   3
HELIX    6   6 LEU A  157  LEU A  164  1                                   8
HELIX    7   7 ASP A  165  LYS A  168  5                                   4
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  ARG A  227  1                                   9
SHEET    1  AA 2 ASP A  32  ILE A  33  0
SHEET    2  AA 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
SHEET    1  AB 7 LYS A  39  TYR A  40  0
SHEET    2  AB 7 LYS A 257  ALA A 258  1  N  ALA A 258   O  LYS A  39
SHEET    3  AB 7 TYR A 191  GLY A 196 -1  O  THR A 193   N  LYS A 257
SHEET    4  AB 7 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5  AB 7 LEU A 141  VAL A 150  1  O  LEU A 141   N  THR A 208
SHEET    6  AB 7 ALA A 116  ASN A 124 -1  O  ALA A 116   N  LEU A 148
SHEET    7  AB 7 TYR A  88  TRP A  97 -1  O  ARG A  89   N  TRP A 123
SHEET    1  AC 6 LYS A  39  TYR A  40  0
SHEET    2  AC 6 LYS A 257  ALA A 258  1  N  ALA A 258   O  LYS A  39
SHEET    3  AC 6 TYR A 191  GLY A 196 -1  O  THR A 193   N  LYS A 257
SHEET    4  AC 6 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5  AC 6 LEU A 141  VAL A 150  1  O  LEU A 141   N  THR A 208
SHEET    6  AC 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  LYS A 149
LINK        ZN    ZN A1262                 NE2 HIS A  96     1555   1555  2.01
LINK        ZN    ZN A1262                 ND1 HIS A 119     1555   1555  2.02
LINK        ZN    ZN A1262                 NE2 HIS A  94     1555   1555  2.06
LINK        ZN    ZN A1262                 N   FB1 A1263     1555   1555  1.87
CISPEP   1 SER A   29    PRO A   30          0         0.29
CISPEP   2 PRO A  201    PRO A  202          0         4.10
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  FB1 A1263
SITE     1 AC2 11 HIS A  94  HIS A  96  HIS A 119  LEU A 141
SITE     2 AC2 11 VAL A 143  LEU A 198  THR A 199  THR A 200
SITE     3 AC2 11 TRP A 209   ZN A1262  GOL A1264
SITE     1 AC3  8 ASN A  62  HIS A  64  ALA A  65  ASN A  67
SITE     2 AC3  8 GLN A  92  HIS A  94  FB1 A1263  HOH A2137
CRYST1   42.432   41.223   72.038  90.00 104.26  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      0.023567  0.000000  0.005990        0.00000
SCALE2      0.000000  0.024258  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014323        0.00000
      
PROCHECK
Go to PROCHECK summary
 References