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PDBsum entry 4bcw

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Lyase PDB id
4bcw
Jmol
Contents
Protein chain
257 a.a.
Ligands
TU0
Metals
_ZN
Waters ×238
HEADER    LYASE                                   03-OCT-12   4BCW
TITLE     CARBONIC ANHYDRASE IX MIMIC IN COMPLEX WITH (E)-2-(5-BROMO-
TITLE    2 2-HYDROXYPHENYL)ETHENESULFONIC ACID
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 4-260;
COMPND   5 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC,
COMPND   6  CARBONIC ANHYDRASE II, CA-II;
COMPND   7 EC: 4.2.1.1;
COMPND   8 ENGINEERED: YES;
COMPND   9 MUTATION: 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: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS    LYASE, SULFOCOUMARIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.TARS,J.LEITANS,A.KAZAKS
REVDAT   1   06-FEB-13 4BCW    0
JRNL        AUTH   K.TARS,D.VULLO,A.KAZAKS,J.LEITANS,A.LENDS,A.GRANDANE,
JRNL        AUTH 2 R.ZALUBOVSKIS,A.SCOZZAFAVA,C.T.SUPURAN
JRNL        TITL   SULFOCOUMARINS (1,2-BENZOXATHIINE-2,2-DIOXIDES): A CLASS OF
JRNL        TITL 2 POTENT AND ISOFORM-SELECTIVE INHIBITORS OF TUMOR-ASSOCIATED
JRNL        TITL 3 CARBONIC ANHYDRASES.
JRNL        REF    J.MED.CHEM.                   V.  56   293 2013
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   23241068
JRNL        DOI    10.1021/JM301625S
REMARK   2
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.6.0117
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) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.28
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.28
REMARK   3   NUMBER OF REFLECTIONS             : 35241
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) : 0.18309
REMARK   3   R VALUE            (WORKING SET) : 0.18114
REMARK   3   FREE R VALUE                     : 0.21924
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 1859
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) : 1.500
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.539
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2484
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.84
REMARK   3   BIN R VALUE           (WORKING SET) : 0.300
REMARK   3   BIN FREE R VALUE SET COUNT          : 119
REMARK   3   BIN FREE R VALUE                    : 0.365
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2086
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 15
REMARK   3   SOLVENT ATOMS            : 238
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 11.9
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.534
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00
REMARK   3    B22 (A**2) : -0.03
REMARK   3    B33 (A**2) : 0.03
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.00
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.084
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.088
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.053
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.430
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2170 ; 0.011 ; 0.020
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2960 ; 1.475 ; 1.955
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   269 ; 6.432 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   101 ;37.785 ;24.752
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   363 ;12.535 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;23.473 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   310 ; 0.103 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1686 ; 0.008 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
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   : 1.20
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 4BCW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-OCT-12.
REMARK 100 THE PDBE ID CODE IS EBI-54306.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-12
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 2
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : MAX II
REMARK 200  BEAMLINE                       : I911-3
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000
REMARK 200  MONOCHROMATOR                  : SI (111) DOUBLE CRYSTAL
REMARK 200  OPTICS                         : RH-COATED TOROIDAL SI
REMARK 200                                   MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35241
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.50
REMARK 200  RESOLUTION RANGE LOW       (A) : 23.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0
REMARK 200  DATA REDUNDANCY                : 2
REMARK 200  R MERGE                    (I) : 0.07
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 7.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.2
REMARK 200  R MERGE FOR SHELL          (I) : 0.32
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 3DC9
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3M AMMONIUM SULPHATE, 100 MM
REMARK 280  TRIS-HCL PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       20.73500
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A  2134     O    HOH A  2231     2546     1.63
REMARK 500
REMARK 500 REMARK: NULL
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    THR A 125   C     LYS A 127   N       0.234
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    ARG A  89   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ARG A  27       57.13   -144.87
REMARK 500    LEU A  57      -52.42   -122.76
REMARK 500    LYS A 111       -1.80     74.18
REMARK 500    PHE A 176       52.46   -148.63
REMARK 500    LYS A 252     -137.60     56.42
REMARK 500    ASN A 253       59.88    -90.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 301  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  96   NE2
REMARK 620 2 HIS A 119   ND1  98.4
REMARK 620 3 HIS A  94   NE2 104.5 111.6
REMARK 620 4 HOH A2121   O   101.4 123.7 113.3
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TU0 A 302
REMARK 900
REMARK 900 RELATED ENTRIES
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: 1A42   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH BRINZOLAMIDE
REMARK 900 RELATED ID: 1AM6   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR: ACETOHYDROXAMATE
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: 1BCD   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH TRIFLUOROMETHANE
REMARK 900  SULPHONAMIDE
REMARK 900 RELATED ID: 1BIC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH THR 200 REPLACED BY
REMARK 900   HIS (T200H) COMPLEX WITH BICARBONATE
REMARK 900 RELATED ID: 1BN1   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1BN3   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1BN4   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1BNM   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1BNN   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: 1BNT   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1BNU   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1BNV   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1BNW   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II INHIBITOR
REMARK 900 RELATED ID: 1BV3   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH UREA
REMARK 900 RELATED ID: 1CA2   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
REMARK 900 RELATED ID: 1CA3   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II) (
REMARK 900  PH 5.7)
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: 1CAI   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH GLU 106 REPLACED BY
REMARK 900   ALA (E106A)
REMARK 900 RELATED ID: 1CAJ   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH GLU 106 REPLACED BY
REMARK 900   ASP (E106D)
REMARK 900 RELATED ID: 1CAK   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH GLU 106 REPLACED BY
REMARK 900   GLN (E106Q)
REMARK 900 RELATED ID: 1CAL   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH THR 199 REPLACED BY
REMARK 900   ALA (T199A)
REMARK 900 RELATED ID: 1CAM   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH THR 199 REPLACED BY
REMARK 900   ALA (T199A) COMPLEX WITH BICARBONATE
REMARK 900 RELATED ID: 1CAN   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH NITRATE
REMARK 900 RELATED ID: 1CAO   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH HYDROGEN SULFIDE
REMARK 900 RELATED ID: 1CAY   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH ACETATE
REMARK 900 RELATED ID: 1CAZ   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH GLU 106 REPLACED BY
REMARK 900   GLN (E106Q) COMPLEX WITH ACETATE
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: 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: 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: 1CIL   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH THE INHIBITOR ETS
REMARK 900 RELATED ID: 1CIM   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH THE INHIBITOR PTS
REMARK 900 RELATED ID: 1CIN   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH THE INHIBITOR MTS
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
REMARK 900  WITH BETA-MERCAPTOETHANOL (BME)
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
REMARK 900  WITH ZINC
REMARK 900 RELATED ID: 1CNG   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II,
REMARK 900  CA2) MUTANT WITH GLU 117 REPLACED BY ALA (E117A)
REMARK 900 RELATED ID: 1CNH   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II,
REMARK 900  CA2) MUTANT WITH GLN 92 REPLACED BY GLU (Q92E)
REMARK 900 RELATED ID: 1CNI   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II,
REMARK 900  CA2) MUTANT WITH GLN 92 REPLACED BY ALA (Q92A)
REMARK 900 RELATED ID: 1CNJ   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II,
REMARK 900  CA2) MUTANT WITH GLN 92 REPLACED BY ASN (Q92N)
REMARK 900 RELATED ID: 1CNK   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA II,
REMARK 900  CA2) MUTANT WITH GLN 92 REPLACED BY LEU (Q92L)
REMARK 900 RELATED ID: 1CNW   RELATED DB: PDB
REMARK 900 RELATED ID: 1CNX   RELATED DB: PDB
REMARK 900 RELATED ID: 1CNY   RELATED DB: PDB
REMARK 900 RELATED ID: 1CRA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH 1,2,4-TRIAZOLE
REMARK 900 RELATED ID: 1CVA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (HCA II) MUTANT WITH THR 199
REMARK 900  REPLACED BY VAL (T199V) (AZIDE-BOUND FORM)
REMARK 900 RELATED ID: 1CVB   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (HCA II) MUTANT WITH THR 199
REMARK 900  REPLACED BY VAL (T199V) (SULFATE-BOUND FORM)
REMARK 900 RELATED ID: 1CVC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH HIS 94 REPLACED BY
REMARK 900  ASP (H94D)
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: 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: 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: 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: 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: 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: 1EOU   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II
REMARK 900  COMPLEXEDWITH AN ANTICONVULSANT SUGAR SULFAMATE
REMARK 900 RELATED ID: 1F2W   RELATED DB: PDB
REMARK 900  THE MECHANISM OF CYANAMIDE HYDRATION CATALYZED BY
REMARK 900  CARBONIC ANHYDRASE II REVEALED BY CRYOGENIC X-RAY
REMARK 900  DIFFRACTION
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: 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: 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: 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: 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: 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: 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: 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: 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: 1G0E   RELATED DB: PDB
REMARK 900  SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH ALA) OF
REMARK 900  HUMANCARBONIC ANHYDRASE II COMPLEXED WITH 4-
REMARK 900  METHYLIMIDAZOLE
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: 1G1D   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N
REMARK 900  -[(2-FLUOROPHENYL)METHYL]-BENZAMIDE
REMARK 900 RELATED ID: 1G3Z   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V)
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: 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: 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: 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: 1G4O   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(
REMARK 900  AMINOSULFONYL)-N-PHENYLMETHYLBENZAMIDE
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: 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: 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: 1H4N   RELATED DB: PDB
REMARK 900  H94N CARBONIC ANHYDRASE II COMPLEXED WITH TRIS
REMARK 900 RELATED ID: 1H9N   RELATED DB: PDB
REMARK 900  H119N CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1H9Q   RELATED DB: PDB
REMARK 900  H119Q CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1HCA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II) (
REMARK 900  PH 6.5)
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: 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: 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: 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: 1HVA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH HIS 94 REPLACED BY
REMARK 900  CYS (H94C)
REMARK 900 RELATED ID: 1I8Z   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH AL-6629 2H-THIENO
REMARK 900  [3,2-E]-1,2-THIAZINE-6-SULFONAMIDE, 2-(3-
REMARK 900  METHOXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1-DIOXIDE
REMARK 900 RELATED ID: 1I90   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH AL-8520 2H-THIENO
REMARK 900  [3,2-E]-1,2-THIAZINE-6-SULFONAMIDE, 4-AMINO-3,4
REMARK 900  -DIHYDRO-2-(3-METHOXYPROPYL)-, 1,1-DIOXIDE, (R)
REMARK 900 RELATED ID: 1I91   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH AL-6619 2H-THIENO
REMARK 900  [3,2-E]-1,2-THIAZINE-6-SULFONAMIDE, 2-(3-
REMARK 900  HYDROXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1-DIOXIDE
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: 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: 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: 1I9O   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(
REMARK 900  AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-
REMARK 900  BENZAMIDE
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]-
REMARK 900  BENZAMIDE
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]-
REMARK 900  BENZAMIDE
REMARK 900 RELATED ID: 1IF4   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH 4-
REMARK 900  FLUOROBENZENESULFONAMIDE
REMARK 900 RELATED ID: 1IF5   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH 2,6-
REMARK 900  DIFLUOROBENZENESULFONAMIDE
REMARK 900 RELATED ID: 1IF6   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH 3,5-
REMARK 900  DIFLUOROBENZENESULFONAMIDE
REMARK 900 RELATED ID: 1IF7   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH (R)-N-(3-INDOL-
REMARK 900  1-YL-2-METHYL-PROPYL)-4-SULFAMOYL-BENZAMIDE
REMARK 900 RELATED ID: 1IF8   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH (S)-N-(3-INDOL-
REMARK 900  1-YL-2-METHYL-PROPYL)-4-SULFAMOYL-BENZAMIDE
REMARK 900 RELATED ID: 1IF9   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEXED WITH N-[2-(1H-INDOL-
REMARK 900  5-YL)-BUTYL]-4-SULFAMOYL-BENZAMIDE
REMARK 900 RELATED ID: 1KWQ   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH INHIBITOR
REMARK 900  2000-07
REMARK 900 RELATED ID: 1KWR   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH INHIBITOR
REMARK 900  0134-36
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: 1LG6   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF HCA II MUTANT T199P
REMARK 900  INCOMPLEX WITH THIOCYANATE
REMARK 900 RELATED ID: 1LGD   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF HCA II MUTANT T199P
REMARK 900  INCOMPLEX WITH BICARBONATE
REMARK 900 RELATED ID: 1LUG   RELATED DB: PDB
REMARK 900  FULL MATRIX ERROR ANALYSIS OF CARBONIC ANHYDRASE
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: 1MOO   RELATED DB: PDB
REMARK 900  SITE SPECIFIC MUTANT (H64A) OF HUMAN CARBONIC ANHYDRASE
REMARK 900   IIAT HIGH RESOLUTION
REMARK 900 RELATED ID: 1MUA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT WITH PRO 202 REPLACED BY
REMARK 900   ALA (P202A)
REMARK 900 RELATED ID: 1OKL   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKL INHIBITOR
REMARK 900  5-DIMETHYLAMINO-NAPHTHALENE-1-SULFONAMIDE
REMARK 900 RELATED ID: 1OKM   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKM INHIBITOR
REMARK 900  4-SULFONAMIDE-[1-(4-AMINOBUTANE)]BENZAMIDE
REMARK 900 RELATED ID: 1OKN   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKN INHIBITOR
REMARK 900  4-SULFONAMIDE-[1-(4-N-(5-FLUORESCEIN THIOUREA)BUTANE
REMARK 900  )]
REMARK 900 RELATED ID: 1OQ5   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II IN COMPLEX WITH NANOMOLAR
REMARK 900  INHIBITOR
REMARK 900 RELATED ID: 1RAY   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH AZIDE
REMARK 900 RELATED ID: 1RAZ   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II COMPLEX WITH BROMIDE
REMARK 900 RELATED ID: 1RZA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II WITH ZINC REPLACED BY COBALT(II
REMARK 900  )
REMARK 900 RELATED ID: 1RZB   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II WITH ZINC REPLACED BY BY COBALT
REMARK 900  (II) AT PH 6.0
REMARK 900 RELATED ID: 1RZC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II WITH ZINC REPLACED BY COPPER(II
REMARK 900  )
REMARK 900 RELATED ID: 1RZD   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II WITH ZINC REPLACED BY MANGANESE(
REMARK 900  II)
REMARK 900 RELATED ID: 1RZE   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II WITH ZINC REPLACED BY NICKEL(II
REMARK 900  )
REMARK 900 RELATED ID: 1T9N   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+
REMARK 900  TRANSFER IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1TB0   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+
REMARK 900  TRANSFER IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1TBT   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+
REMARK 900  TRANSFER IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1TE3   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+
REMARK 900  TRANSFER IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1TEQ   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+
REMARK 900  TRANSFER IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1TEU   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+
REMARK 900  TRANSFER IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1TG3   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+
REMARK 900  TRANSFER IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1TG9   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+
REMARK 900  TRANSFER IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1TH9   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+
REMARK 900  TRANSFER IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1THK   RELATED DB: PDB
REMARK 900  EFFECT OF SHUTTLE LOCATION AND PH ENVIRONMENT ON H+
REMARK 900  TRANSFER IN HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 1TTM   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH 667-COUMATE
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: 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: 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: 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: 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: 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: 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: 1XEG   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II
REMARK 900  COMPLEXEDWITH AN ACETATE ION
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: 1YDA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE)(HCA II)
REMARK 900  MUTANT WITH LEU 198 REPLACED BY GLU (L198E) COMPLEXED
REMARK 900   WITH TRANSITION STATE ANALOG ACETAZOLAMIDE
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
REMARK 900   WITH TRANSITION STATE ANALOG ACETAZOLAMIDE
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: 1YDD   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE)(HCA II)
REMARK 900  MUTANT WITH LEU 198 REPLACED BY ARG (L198R) COMPLEXED
REMARK 900   WITH TRANSITION STATE ANALOG ACETAZOLAMIDE
REMARK 900 RELATED ID: 1YO0   RELATED DB: PDB
REMARK 900  PROTON TRANSFER FROM HIS200 IN HUMAN CARBONIC ANHYDRASE
REMARK 900   II
REMARK 900 RELATED ID: 1YO1   RELATED DB: PDB
REMARK 900  PROTON TRANSFER FROM HIS200 IN HUMAN CARBONIC ANHYDRASE
REMARK 900   II
REMARK 900 RELATED ID: 1YO2   RELATED DB: PDB
REMARK 900  PROTON TRANSFER FROM HIS200 IN HUMAN CARBONIC ANHYDRASE
REMARK 900   II
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: 1ZE8   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II IN COMPLEX WITH A MEMBRANE-
REMARK 900  IMPERMEANTSULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 1ZFK   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II IN COMPLEX WITH N-4-
REMARK 900  SULFONAMIDPHENYL-N'-4-METHYLBENZOSULFONYLUREASE AS
REMARK 900  SULFONAMIDE INHIBITOR
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: 1ZGE   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II IN COMPLEX WITH P-SULFONAMIDO-O
REMARK 900  ,O'-DICHLOROANILINE AS SULFONAMIDE INHIBITOR
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: 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: 1ZSA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT E117Q, APO FORM
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: 1ZSC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II MUTANT E117Q, HOLO FORM
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: 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: 2AX2   RELATED DB: PDB
REMARK 900  PRODUCTION AND X-RAY CRYSTALLOGRAPHIC ANALYSIS OF
REMARK 900  FULLYDEUTERATED HUMAN CARBONIC ANHYDRASE II
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: 2CBA   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (50 MM TRIS, 3 M AMMONIUM
REMARK 900  SULFATE, PH 7.8)
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: 2CBC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (50 MM TRIS, 3 M AMMONIUM
REMARK 900  SULFATE, 0.2 FORMATE, PH 7.6)
REMARK 900 RELATED ID: 2CBD   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (2.4 M AMMONIUM SULFATE, 0.3
REMARK 900  M SODIUM BISULFITE, PH 7.3)
REMARK 900 RELATED ID: 2CBE   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (50 MM TRIS, 3 M AMMONIUM
REMARK 900  SULFATE, 2MM DIPICOLINATE, PH 7.8)
REMARK 900 RELATED ID: 2EU2   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH NOVEL
REMARK 900  INHIBITORS
REMARK 900 RELATED ID: 2EU3   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH NOVEL
REMARK 900  INHIBITORS
REMARK 900 RELATED ID: 2EZ7   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE ACTIVATORS. ACTIVATION OF ISOZYMES I,
REMARK 900  II,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: 2FMG   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE ACTIVATORS. ACTIVATION OF ISOFORMS I,
REMARK 900  II,IV, VA, VII AND XIV WITH L- AND D-
REMARK 900  PHENYLALANINE ANDCRYSTALLOGRAPHIC ANALYSIS OF THEIR ADDUCTS
REMARK 900   WITH ISOZYMEII: STEROSPECIFIC RECOGNITION WITHIN THE
REMARK 900  ACTIVE SITE OF ANENZYME AND ITS CONSEQUENCES FOR THE
REMARK 900  DRUG DESIGN, STRUCTUREWITH L-PHENYLALANINE
REMARK 900 RELATED ID: 2FMZ   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE ACTIVATORS. ACTIVATION OF ISOFORMS I,
REMARK 900  II,IV, VA, VII AND XIV WITH L- AND D-
REMARK 900  PHENYLALANINE,STRUCTURE WITH D-PHENYLALANINE.
REMARK 900 RELATED ID: 2FOQ   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH TWO-
REMARK 900  PRONGINHIBITORS
REMARK 900 RELATED ID: 2FOS   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH TWO-
REMARK 900  PRONGINHIBITORS
REMARK 900 RELATED ID: 2FOU   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH TWO-
REMARK 900  PRONGINHIBITORS
REMARK 900 RELATED ID: 2FOV   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH TWO-
REMARK 900  PRONGINHIBITORS
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: 2H4N   RELATED DB: PDB
REMARK 900  H94N CARBONIC ANHYDRASE II COMPLEXED WITH ACETAZOLAMIDE
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: 2VVA   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE IN COMPLEX WITH CO2
REMARK 900 RELATED ID: 2VVB   RELATED DB: PDB
REMARK 900  HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH BICARBONATE
REMARK 900 RELATED ID: 2WD2   RELATED DB: PDB
REMARK 900  A CHIMERIC MICROTUBULE DISRUPTOR WITH EFFICACY ON A
REMARK 900  TAXANE RESISTANT CELL LINE
REMARK 900 RELATED ID: 2WD3   RELATED DB: PDB
REMARK 900  HIGHLY POTENT FIRST EXAMPLES OF DUAL AROMATASE-STEROID
REMARK 900  SULFATASE INHIBITORS BASED ON A BIPHENYL TEMPLATE
REMARK 900 RELATED ID: 2WEG   RELATED DB: PDB
REMARK 900  THERMODYNAMIC OPTIMISATION OF CARBONIC ANHYDRASE FRAGMENT
REMARK 900  INHIBITORS
REMARK 900 RELATED ID: 2WEH   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
REMARK 900 RELATED ID: 2X7S   RELATED DB: PDB
REMARK 900  STRUCTURES OF HUMAN CARBONIC ANHYDRASE II INHIBITOR
REMARK 900  COMPLEXES REVEAL A SECOND BINDING SITE FOR STEROIDAL
REMARK 900  AND NON-STEROIDAL INHIBITORS.
REMARK 900 RELATED ID: 2X7T   RELATED DB: PDB
REMARK 900  STRUCTURES OF HUMAN CARBONIC ANHYDRASE II INHIBITOR
REMARK 900  COMPLEXES REVEAL A SECOND BINDING SITE FOR STEROIDAL
REMARK 900  AND NON-STEROIDAL INHIBITORS.
REMARK 900 RELATED ID: 2X7U   RELATED DB: PDB
REMARK 900  STRUCTURES OF HUMAN CARBONIC ANHYDRASE II INHIBITOR
REMARK 900  COMPLEXES REVEAL A SECOND BINDING SITE FOR STEROIDAL
REMARK 900  AND NON-STEROIDAL INHIBITORS.
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: 4CA2   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II)
REMARK 900 RELATED ID: 4CAC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE FORM C (PH 6)
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: 5CAC   RELATED DB: PDB
REMARK 900  CARBONIC ANHYDRASE FORM C COMPLEX WITH HYDROGEN SULFITE
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: 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: 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)
DBREF  4BCW A    4   261  UNP    P00918   CAH2_HUMAN       4    260
SEQADV 4BCW SER A   65  UNP  P00918    ALA    65 ENGINEERED MUTATION
SEQADV 4BCW GLN A   67  UNP  P00918    ASN    67 ENGINEERED MUTATION
SEQRES   1 A  257  HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU HIS TRP
SEQRES   2 A  257  HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG GLN SER
SEQRES   3 A  257  PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR ASP PRO
SEQRES   4 A  257  SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN ALA THR
SEQRES   5 A  257  SER LEU ARG ILE LEU ASN ASN GLY HIS SER PHE GLN VAL
SEQRES   6 A  257  GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU LYS GLY
SEQRES   7 A  257  GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN PHE HIS
SEQRES   8 A  257  PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER GLU HIS
SEQRES   9 A  257  THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU HIS LEU
SEQRES  10 A  257  VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY LYS ALA
SEQRES  11 A  257  VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY ILE PHE
SEQRES  12 A  257  LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN LYS VAL
SEQRES  13 A  257  VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY LYS SER
SEQRES  14 A  257  ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU LEU PRO
SEQRES  15 A  257  GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER LEU THR
SEQRES  16 A  257  THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE VAL LEU
SEQRES  17 A  257  LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL LEU LYS
SEQRES  18 A  257  PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU PRO GLU
SEQRES  19 A  257  GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN PRO LEU
SEQRES  20 A  257  LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A 301       1
HET    TU0  A 302      14
HETNAM     TU0 (E)-2-(5-BROMO-2-HYDROXYPHENYL)
HETNAM   2 TU0  ETHENESULFONIC ACID
HETNAM      ZN ZINC ION
FORMUL   2  TU0    C8 H7 BR O4 S
FORMUL   3   ZN    ZN 2+
FORMUL   4  HOH   *238(H2 O)
HELIX    1   1 HIS A   15  ASP A   19  5                                   5
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 6 LYS A  39  TYR A  40  0
SHEET    2  AB 6 LYS A 257  ALA A 258  1  N  ALA A 258   O  LYS A  39
SHEET    3  AB 6 TYR A 191  GLY A 196 -1  O  THR A 193   N  LYS A 257
SHEET    4  AB 6 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5  AB 6 LEU A 141  VAL A 150  1  O  LEU A 141   N  THR A 208
SHEET    6  AB 6 ILE A 216  VAL A 218 -1  O  ILE A 216   N  LYS A 149
SHEET    1  AC 9 LYS A  39  TYR A  40  0
SHEET    2  AC 9 LYS A 257  ALA A 258  1  N  ALA A 258   O  LYS A  39
SHEET    3  AC 9 TYR A 191  GLY A 196 -1  O  THR A 193   N  LYS A 257
SHEET    4  AC 9 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5  AC 9 LEU A 141  VAL A 150  1  O  LEU A 141   N  THR A 208
SHEET    6  AC 9 ALA A 116  ASN A 124 -1  O  ALA A 116   N  LEU A 148
SHEET    7  AC 9 TYR A  88  TRP A  97 -1  O  ARG A  89   N  TRP A 123
SHEET    8  AC 9 VAL A  78  GLY A  81 -1  O  LEU A  79   N  TYR A  88
SHEET    9  AC 9 LEU A  47  SER A  50 -1  O  SER A  48   N  LYS A  80
SHEET    1  AD10 LYS A  39  TYR A  40  0
SHEET    2  AD10 LYS A 257  ALA A 258  1  N  ALA A 258   O  LYS A  39
SHEET    3  AD10 TYR A 191  GLY A 196 -1  O  THR A 193   N  LYS A 257
SHEET    4  AD10 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5  AD10 LEU A 141  VAL A 150  1  O  LEU A 141   N  THR A 208
SHEET    6  AD10 ALA A 116  ASN A 124 -1  O  ALA A 116   N  LEU A 148
SHEET    7  AD10 TYR A  88  TRP A  97 -1  O  ARG A  89   N  TRP A 123
SHEET    8  AD10 PHE A  66  PHE A  70 -1  O  PHE A  66   N  PHE A  95
SHEET    9  AD10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   10  AD10 SER A 173  ASP A 175  1  O  ALA A 174   N  ILE A  59
SHEET    1  AE 2 ILE A 216  VAL A 218  0
SHEET    2  AE 2 LEU A 141  VAL A 150 -1  O  PHE A 147   N  ILE A 216
LINK        ZN    ZN A 301                 NE2 HIS A  96     1555   1555  2.06
LINK        ZN    ZN A 301                 ND1 HIS A 119     1555   1555  2.05
LINK        ZN    ZN A 301                 NE2 HIS A  94     1555   1555  1.93
LINK        ZN    ZN A 301                 O   HOH A2121     1555   1555  1.87
CISPEP   1 SER A   29    PRO A   30          0        -3.20
CISPEP   2 PRO A  201    PRO A  202          0         9.94
SITE     1 AC1  5 HIS A  94  HIS A  96  HIS A 119  TU0 A 302
SITE     2 AC1  5 HOH A2121
SITE     1 AC2 12 GLN A  92  HIS A  94  HIS A 119  PHE A 131
SITE     2 AC2 12 VAL A 143  LEU A 198  THR A 199  THR A 200
SITE     3 AC2 12 TRP A 209   ZN A 301  HOH A2121  HOH A2204
CRYST1   42.180   41.470   72.000  90.00 104.06  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      0.023708  0.000000  0.005937        0.00000
SCALE2      0.000000  0.024114  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014318        0.00000
      
PROCHECK
Go to PROCHECK summary
 References