spacer
spacer

PDBsum entry 3bl1

Go to PDB code: 
Top Page protein ligands metals links
Lyase PDB id
3bl1
Jmol
Contents
Protein chain
256 a.a.
Ligands
BL1
Metals
_ZN
_HG
Waters ×163
HEADER    LYASE                                   10-DEC-07   3BL1
TITLE     CARBONIC ANHYDRASE INHIBITORS. SULFONAMIDE DIURETICS
TITLE    2 REVISITED OLD LEADS FOR NEW APPLICATIONS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE II, CARBONATE DEHYDRATASE II,
COMPND   5 CA-II, CARBONIC ANHYDRASE C;
COMPND   6 EC: 4.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN
KEYWDS    CARBONIC ANHYDRASE, INHIBITORS, CRYSTAL STRUCTURE,
KEYWDS   2 DIURETICS, ACETYLATION, CYTOPLASM, DISEASE MUTATION, LYASE,
KEYWDS   3 METAL-BINDING, POLYMORPHISM, ZINC, LYASE(OXO-ACID)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.TEMPERINI,A.CECCHI,C.T.SUPURAN
REVDAT   2   24-FEB-09 3BL1    1       VERSN
REVDAT   1   01-JUL-08 3BL1    0
JRNL        AUTH   C.TEMPERINI,A.CECCHI,A.SCOZZAFAVA,C.T.SUPURAN
JRNL        TITL   CARBONIC ANHYDRASE INHIBITORS. INTERACTION OF
JRNL        TITL 2 INDAPAMIDE AND RELATED DIURETICS WITH 12 MAMMALIAN
JRNL        TITL 3 ISOZYMES AND X-RAY CRYSTALLOGRAPHIC STUDIES FOR
JRNL        TITL 4 THE INDAPAMIDE-ISOZYME II ADDUCT.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  18  2567 2008
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   18374572
JRNL        DOI    10.1016/J.BMCL.2008.03.051
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
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) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.0
REMARK   3   NUMBER OF REFLECTIONS             : 11494
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) : 0.228
REMARK   3   R VALUE            (WORKING SET) : 0.224
REMARK   3   FREE R VALUE                     : 0.299
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 621
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) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 822
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910
REMARK   3   BIN FREE R VALUE SET COUNT          : 39
REMARK   3   BIN FREE R VALUE                    : 0.4410
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2042
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 26
REMARK   3   SOLVENT ATOMS            : 163
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.40
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.11000
REMARK   3    B22 (A**2) : -0.10000
REMARK   3    B33 (A**2) : 0.09000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.25000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.472
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.298
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.218
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.700
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.914
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.846
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2129 ; 0.015 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2894 ; 1.876 ; 1.962
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   256 ; 7.226 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    98 ;37.286 ;24.694
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   349 ;19.309 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;19.755 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   301 ; 0.112 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1645 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1066 ; 0.233 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1367 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   172 ; 0.207 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.064 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    44 ; 0.264 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.204 ; 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):  1311 ; 0.672 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2058 ; 1.098 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   959 ; 1.802 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   835 ; 2.575 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
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 3BL1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-07.
REMARK 100 THE RCSB ID CODE IS RCSB045651.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-NOV-07
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : SEALED TUBE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : OXFORD DIFFRACTION ENHANCED
REMARK 200                                   ULTRA
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : CAPILLARY
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : OXFORD SAPPHIRE CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSALISRED OXFORD
REMARK 200                                   DIFFRACTION2006
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12582
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7
REMARK 200  DATA REDUNDANCY                : 2.000
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.14000
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.30000
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS.HCL PH 7.7-7.8 , SODIUM 4-
REMARK 280  (HYDROXYMERCURY)BENZOATE , VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 277K
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       20.66000
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     SER A     2
REMARK 465     HIS A     3
REMARK 465     LYS A   261
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   NZ   LYS A   127     O    HOH A   460              2.06
REMARK 500   O    HOH A   361     O    HOH A   459              2.09
REMARK 500   O    HOH A   314     O    HOH A   347              2.11
REMARK 500   O    HOH A   446     O    HOH A   449              2.19
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  44   CA  -  CB  -  CG  ANGL. DEV. =  14.5 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    LYS A  76      -64.93   -131.35
REMARK 500    LYS A 111       -2.70     73.04
REMARK 500    MET A 241       89.30    -68.44
REMARK 500    ASN A 253      -35.76     88.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 447        DISTANCE =  5.21 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 102.2
REMARK 620 3 HIS A 119   ND1 113.9 101.9
REMARK 620 4 BL1 A 300   NAS 108.9 121.1 108.8
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 262
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 263
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BL1 A 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EU2   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH AN ANALOGUE COMPOUND
REMARK 900 RELATED ID: 2EU3   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH AN ANALOGUE COMPOUND
REMARK 900 RELATED ID: 3BL0   RELATED DB: PDB
DBREF  3BL1 A    1   261  UNP    P00918   CAH2_HUMAN       1    260
SEQRES   1 A  260  MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES   2 A  260  GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES   3 A  260  ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES   4 A  260  TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES   5 A  260  GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES   6 A  260  PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES   7 A  260  LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES   8 A  260  GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES   9 A  260  SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES  10 A  260  LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES  11 A  260  GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 A  260  GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES  13 A  260  GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES  14 A  260  GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES  15 A  260  LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES  16 A  260  SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES  17 A  260  ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES  18 A  260  VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES  19 A  260  GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES  20 A  260  GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A 262       1
HET     HG  A 263       1
HET    BL1  A 300      24
HETNAM      ZN ZINC ION
HETNAM      HG MERCURY (II) ION
HETNAM     BL1 4-CHLORO-N-[(2S)-2-METHYL-2,3-DIHYDRO-1H-INDOL-1-YL]-
HETNAM   2 BL1  3-SULFAMOYLBENZAMIDE
HETSYN     BL1 INDAPAMIDE
FORMUL   2   ZN    ZN 2+
FORMUL   3   HG    HG 2+
FORMUL   4  BL1    C16 H16 CL N3 O3 S
FORMUL   5  HOH   *163(H2 O)
HELIX    1   1 PHE A   20  GLY A   25  5                                   6
HELIX    2   2 ASP A  130  VAL A  135  1                                   6
HELIX    3   3 LYS A  154  GLY A  156  5                                   3
HELIX    4   4 LEU A  157  LEU A  164  1                                   8
HELIX    5   5 ASP A  165  LYS A  168  5                                   4
HELIX    6   6 ASP A  180  LEU A  185  5                                   6
HELIX    7   7 SER A  219  ARG A  227  1                                   9
SHEET    1   A 2 ASP A  32  ILE A  33  0
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
SHEET    1   B 9 LYS A  39  TYR A  40  0
SHEET    2   B 9 LYS A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B 9 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4   B 9 VAL A 207  VAL A 218 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B 9 LEU A 141  VAL A 150  1  N  LYS A 149   O  VAL A 218
SHEET    6   B 9 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 146
SHEET    7   B 9 TYR A  88  TRP A  97 -1  N  ILE A  91   O  VAL A 121
SHEET    8   B 9 VAL A  78  GLY A  81 -1  N  LEU A  79   O  TYR A  88
SHEET    9   B 9 LEU A  47  SER A  50 -1  N  SER A  48   O  LYS A  80
SHEET    1   C10 LYS A  39  TYR A  40  0
SHEET    2   C10 LYS A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   C10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4   C10 VAL A 207  VAL A 218 -1  O  VAL A 207   N  GLY A 196
SHEET    5   C10 LEU A 141  VAL A 150  1  N  LYS A 149   O  VAL A 218
SHEET    6   C10 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 146
SHEET    7   C10 TYR A  88  TRP A  97 -1  N  ILE A  91   O  VAL A 121
SHEET    8   C10 PHE A  66  PHE A  70 -1  N  PHE A  70   O  ILE A  91
SHEET    9   C10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   10   C10 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59
LINK         NE2 HIS A  94                ZN    ZN A 262     1555   1555  2.06
LINK         NE2 HIS A  96                ZN    ZN A 262     1555   1555  2.02
LINK         ND1 HIS A 119                ZN    ZN A 262     1555   1555  1.96
LINK        ZN    ZN A 262                 NAS BL1 A 300     1555   1555  2.15
CISPEP   1 SER A   29    PRO A   30          0        -2.84
CISPEP   2 PRO A  201    PRO A  202          0         7.59
SITE     1 AC1  3 HIS A  94  HIS A  96  HIS A 119
SITE     1 AC2  4 GLN A 137  GLU A 205  CYS A 206  HOH A 420
SITE     1 AC3  9 HIS A  64  GLN A  92  HIS A  94  HIS A  96
SITE     2 AC3  9 HIS A 119  PHE A 131  LEU A 198  THR A 199
SITE     3 AC3  9 TRP A 209
CRYST1   42.050   41.320   72.250  90.00 104.29  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      0.023781  0.000000  0.006057        0.00000
SCALE2      0.000000  0.024201  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014283        0.00000
      
PROCHECK
Go to PROCHECK summary
 References