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PDBsum entry 3vbd

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Lyase/lyase inhibitor PDB id
3vbd
Jmol
Contents
Protein chain
258 a.a.
Ligands
0FZ
MBO ×2
GOL ×2
Metals
_ZN
Waters ×430
HEADER    LYASE/LYASE INHIBITOR                   02-JAN-12   3VBD
TITLE     COMPLEX OF HUMAN CARBONIC ANHYDRASE II WITH 4-(6-METHOXY-3,4-
TITLE    2 DIHYDROISOQUINOLIN-1-YL)BENZENESULFONAMIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC,
COMPND   5 CARBONIC ANHYDRASE II, CA-II;
COMPND   6 EC: 4.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606
KEYWDS    LYASE-LYASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.MADER,J.BRYNDA,P.REZACOVA
REVDAT   3   27-JUN-12 3VBD    1       JRNL
REVDAT   2   11-APR-12 3VBD    1       JRNL
REVDAT   1   04-APR-12 3VBD    0
JRNL        AUTH   R.GITTO,F.M.DAMIANO,P.MADER,L.DE LUCA,S.FERRO,C.T.SUPURAN,
JRNL        AUTH 2 D.VULLO,J.BRYNDA,P.REZACOVA,A.CHIMIRRI
JRNL        TITL   SYNTHESIS, STRUCTURE-ACTIVITY RELATIONSHIP STUDIES, AND
JRNL        TITL 2 X-RAY CRYSTALLOGRAPHIC ANALYSIS OF ARYLSULFONAMIDES AS
JRNL        TITL 3 POTENT CARBONIC ANHYDRASE INHIBITORS.
JRNL        REF    J.MED.CHEM.                   V.  55  3891 2012
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   22443141
JRNL        DOI    10.1021/JM300112W
REMARK   2
REMARK   2 RESOLUTION.    1.05 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   CROSS-VALIDATION METHOD           : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.134
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.160
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 5556
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 109842
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2051
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 55
REMARK   3   SOLVENT ATOMS      : 430
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL
REMARK   3   NUMBER OF RESTRAINTS                     : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.015
REMARK   3   ANGLE DISTANCES                      (A) : 0.036
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3VBD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-12.
REMARK 100 THE RCSB ID CODE IS RCSB069831.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : BESSY
REMARK 200  BEAMLINE                       : 14.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.915
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 109951
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.050
REMARK 200  RESOLUTION RANGE LOW       (A) : 16.760
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : 0.05300
REMARK 200  R SYM                      (I) : 0.05300
REMARK 200   FOR THE DATA SET  : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.08
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.41300
REMARK 200  R SYM FOR SHELL            (I) : 0.41300
REMARK 200   FOR SHELL         : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC 5.5.0110
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3 M AMMONIUM SULFATE, 50 MM TRIS-HCL,
REMARK 280  2 MM 4-(HYDROXYMERCURI)BENZOATE, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 291K
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       20.59000
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     SER A  1002
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     LYS A1009    CE   NZ
REMARK 470     LYS A1045    CD   CE   NZ
REMARK 470     LYS A1261    CD   CE   NZ
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    LYS A1261   C     LYS A1261   OXT     0.149
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 A1027   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    TYR A1051   CB  -  CG  -  CD2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    TYR A1051   CB  -  CG  -  CD1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    LEU A1060   C   -  N   -  CA  ANGL. DEV. =  18.1 DEGREES
REMARK 500    GLU A1069   CA  -  C   -  N   ANGL. DEV. = -13.6 DEGREES
REMARK 500    TYR A1088   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG A1182   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    PHE A1226   CB  -  CG  -  CD2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    PHE A1226   CB  -  CG  -  CD1 ANGL. DEV. =   4.5 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    ASN A1011       12.79   -140.88
REMARK 500    ARG A1027       59.12   -143.61
REMARK 500    ALA A1077       78.18     56.66
REMARK 500    GLU A1106      -60.40    -94.05
REMARK 500    LYS A1111       -2.72     73.66
REMARK 500    PHE A1176       78.22   -153.55
REMARK 500    ASN A1244       48.55    -94.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 LEU A 1057     ARG A 1058                 -146.53
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 A6156        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH A6275        DISTANCE =  8.24 ANGSTROMS
REMARK 525    HOH A6281        DISTANCE =  8.50 ANGSTROMS
REMARK 525    HOH A6285        DISTANCE =  9.51 ANGSTROMS
REMARK 525    HOH A6327        DISTANCE =  6.36 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 A2001  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 0FZ A2002   NAC
REMARK 620 2 HIS A1094   NE2 110.8
REMARK 620 3 HIS A1119   ND1 115.3 112.6
REMARK 620 4 HIS A1096   NE2 114.2 104.5  98.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             MBO A2003  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1206   SG
REMARK 620 2 MBO A2003   CE1 177.6
REMARK 620 N                    1
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 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0FZ A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MBO A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MBO A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2006
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3V7X   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH DIFFERENT INHIBITOR
DBREF  3VBD A 1002  1261  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  A2001       1
HET    0FZ  A2002      34
HET    MBO  A2003      20
HET    MBO  A2004      10
HET    GOL  A2005       6
HET    GOL  A2006       6
HETNAM      ZN ZINC ION
HETNAM     0FZ 4-(6-METHOXY-3,4-DIHYDROISOQUINOLIN-1-YL)
HETNAM   2 0FZ  BENZENESULFONAMIDE
HETNAM     MBO MERCURIBENZOIC ACID
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2   ZN    ZN 2+
FORMUL   3  0FZ    C16 H16 N2 O3 S
FORMUL   4  MBO    2(C7 H5 HG O2)
FORMUL   6  GOL    2(C3 H8 O3)
FORMUL   8  HOH   *430(H2 O)
HELIX    1   1 GLY A 1012  ASP A 1019  5                                   8
HELIX    2   2 PHE A 1020  GLY A 1025  5                                   6
HELIX    3   3 LYS A 1127  GLY A 1129  5                                   3
HELIX    4   4 ASP A 1130  VAL A 1135  1                                   6
HELIX    5   5 LYS A 1154  GLY A 1156  5                                   3
HELIX    6   6 LEU A 1157  LEU A 1164  1                                   8
HELIX    7   7 ASP A 1165  LYS A 1168  5                                   4
HELIX    8   8 ASP A 1180  LEU A 1185  5                                   6
HELIX    9   9 SER A 1219  ARG A 1227  1                                   9
SHEET    1   A 2 ASP A1032  ILE A1033  0
SHEET    2   A 2 THR A1108  VAL A1109  1  O  THR A1108   N  ILE A1033
SHEET    1   B10 LYS A1039  TYR A1040  0
SHEET    2   B10 LYS A1257  ALA A1258  1  O  ALA A1258   N  LYS A1039
SHEET    3   B10 TYR A1191  GLY A1196 -1  N  THR A1193   O  LYS A1257
SHEET    4   B10 VAL A1207  LEU A1212 -1  O  VAL A1207   N  GLY A1196
SHEET    5   B10 LEU A1141  VAL A1150  1  N  GLY A1145   O  LEU A1212
SHEET    6   B10 ALA A1116  ASN A1124 -1  N  LEU A1118   O  ILE A1146
SHEET    7   B10 TYR A1088  TRP A1097 -1  N  HIS A1094   O  HIS A1119
SHEET    8   B10 PHE A1066  PHE A1070 -1  N  VAL A1068   O  PHE A1093
SHEET    9   B10 SER A1056  ASN A1061 -1  N  LEU A1057   O  GLU A1069
SHEET   10   B10 SER A1173  ASP A1175 -1  O  ALA A1174   N  ILE A1059
SHEET    1   C 6 LYS A1045  SER A1050  0
SHEET    2   C 6 VAL A1078  GLY A1082 -1  O  LYS A1080   N  SER A1048
SHEET    3   C 6 TYR A1088  TRP A1097 -1  O  TYR A1088   N  LEU A1079
SHEET    4   C 6 ALA A1116  ASN A1124 -1  O  HIS A1119   N  HIS A1094
SHEET    5   C 6 LEU A1141  VAL A1150 -1  O  ILE A1146   N  LEU A1118
SHEET    6   C 6 ILE A1216  VAL A1218  1  O  ILE A1216   N  PHE A1147
LINK        ZN    ZN A2001                 NAC 0FZ A2002     1555   1555  1.92
LINK         NE2 HIS A1094                ZN    ZN A2001     1555   1555  1.98
LINK         ND1 HIS A1119                ZN    ZN A2001     1555   1555  2.00
LINK         NE2 HIS A1096                ZN    ZN A2001     1555   1555  2.03
LINK         SG ACYS A1206                HG  AMBO A2003     1555   1555  2.32
CISPEP   1 SER A 1029    PRO A 1030          0        -1.37
CISPEP   2 PRO A 1201    PRO A 1202          0         9.06
SITE     1 AC1  4 HIS A1094  HIS A1096  HIS A1119  0FZ A2002
SITE     1 AC2 14 ILE A1091  GLN A1092  HIS A1094  HIS A1096
SITE     2 AC2 14 HIS A1119  VAL A1121  PHE A1131  LEU A1198
SITE     3 AC2 14 THR A1199  THR A1200   ZN A2001  GOL A2006
SITE     4 AC2 14 HOH A6205  HOH A6350
SITE     1 AC3 11 VAL A1135  GLN A1136  GLN A1137  PRO A1138
SITE     2 AC3 11 GLU A1205  CYS A1206  HOH A6162  HOH A6194
SITE     3 AC3 11 HOH A6212  HOH A6255  HOH A6401
SITE     1 AC4  6 HIS A1004  ASN A1062  HIS A1064  LYS A1170
SITE     2 AC4  6 HOH A6168  HOH A6308
SITE     1 AC5  9 TYR A1114  LYS A1149  PRO A1215  HOH A6021
SITE     2 AC5  9 HOH A6136  HOH A6241  HOH A6348  HOH A6411
SITE     3 AC5  9 HOH A6421
SITE     1 AC6 11 ASN A1062  HIS A1064  ALA A1065  ASN A1067
SITE     2 AC6 11 GLN A1092  HIS A1094  0FZ A2002  HOH A6146
SITE     3 AC6 11 HOH A6157  HOH A6254  HOH A6350
CRYST1   42.010   41.180   71.760  90.00 104.33  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      0.023804  0.000000  0.006081        0.00000
SCALE2      0.000000  0.024284  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014383        0.00000
      
PROCHECK
Go to PROCHECK summary
 References