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PDBsum entry 1keq

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Lyase PDB id
1keq
Jmol
Contents
Protein chains
238 a.a. *
Ligands
4MZ ×5
ACY ×3
Metals
__K
_ZN ×2
Waters ×471
* Residue conservation analysis
HEADER    LYASE                                   16-NOV-01   1KEQ
TITLE     CRYSTAL STRUCTURE OF F65A/Y131C CARBONIC ANHYDRASE V,
TITLE    2 COVALENTLY MODIFIED WITH 4-CHLOROMETHYLIMIDAZOLE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: F65A/Y131C-MI CARBONIC ANHYDRASE V;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: CARBONIC ANHYDRASE VC;
COMPND   5 EC: 4.2.1.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 GENE: MCA5C;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET31 T7
KEYWDS    PROTON TRANSFER, ENGINEERED RESIDUE, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.M.JUDE,S.K.WRIGHT,C.TU,D.N.SILVERMAN,R.E.VIOLA,
AUTHOR   2 D.W.CHRISTIANSON
REVDAT   2   24-FEB-09 1KEQ    1       VERSN
REVDAT   1   06-MAR-02 1KEQ    0
JRNL        AUTH   K.M.JUDE,S.K.WRIGHT,C.TU,D.N.SILVERMAN,R.E.VIOLA,
JRNL        AUTH 2 D.W.CHRISTIANSON
JRNL        TITL   CRYSTAL STRUCTURE OF F65A/Y131C-METHYLIMIDAZOLE
JRNL        TITL 2 CARBONIC ANHYDRASE V REVEALS ARCHITECTURAL
JRNL        TITL 3 FEATURES OF AN ENGINEERED PROTON SHUTTLE.
JRNL        REF    BIOCHEMISTRY                  V.  41  2485 2002
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   11851394
JRNL        DOI    10.1021/BI015808Q
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.N.EARNHARDT,S.K.WRIGHT,M.QIAN,C.TU,P.J.LAIPIS,
REMARK   1  AUTH 2 R.E.VIOLA,D.N.SILVERMAN
REMARK   1  TITL   INTRODUCTION OF HISTIDINE ANALOGS LEADS TO
REMARK   1  TITL 2 ENHANCED PROTON TRANSFER IN CARBONIC ANHYDRASE V
REMARK   1  REF    ARCH.BIOCHEM.BIOPHYS.         V. 361   264 1999
REMARK   1  REFN                   ISSN 0003-9861
REMARK   1  DOI    10.1006/ABBI.1998.0984
REMARK   1 REFERENCE 2
REMARK   1  AUTH   P.A.BORIACK-SJODIN,R.W.HECK,P.J.LAIPIS,
REMARK   1  AUTH 2 D.N.SILVERMAN,D.W.CHRISTIANSON
REMARK   1  TITL   STRUCTURE DETERMINATION OF MURINE MITOCHONDRIAL
REMARK   1  TITL 2 CARBONIC ANHYDRASE V AT 2.45-A RESOLUTION:
REMARK   1  TITL 3 IMPLICATIONS FOR CATALYTIC PROTON TRANSFER AND
REMARK   1  TITL 4 INHIBITOR DESIGN.
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  92 10949 1995
REMARK   1  REFN                   ISSN 0027-8424
REMARK   2
REMARK   2 RESOLUTION.    1.88 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : EXAMPLES OF  STEREOCHEMISTRY TARGET VALUES
REMARK   3                      (MMCIF ITEM _REFINE.NDB_STEREOCHEMISTRY_
REMARK   3                      TARGET_VALUES) EXAMPLE 1: ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.88
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.56
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 253283.340
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.4
REMARK   3   NUMBER OF REFLECTIONS             : 45225
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 SET) : 0.185
REMARK   3   FREE R VALUE                     : 0.217
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1808
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.88
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.99
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.20
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6651
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200
REMARK   3   BIN FREE R VALUE                    : 0.2340
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.90
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 273
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3804
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 31
REMARK   3   SOLVENT ATOMS            : 481
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 16.50
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.00
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.38000
REMARK   3    B22 (A**2) : -3.52000
REMARK   3    B33 (A**2) : 3.90000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -1.16000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19
REMARK   3   ESD FROM SIGMAA              (A) : 0.13
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.23
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.13
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.90
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.81
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.250 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.860 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.850 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.630 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.36
REMARK   3   BSOL        : 50.04
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : MYTOPPAR:ACY.PARAM
REMARK   3  PARAMETER FILE  5  : MYTOPPAR:CMI.PARAM
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : MYTOPPAR:ACY.TOP
REMARK   3  TOPOLOGY FILE  3   : MYTOPPAR:CMI.TOP
REMARK   3  TOPOLOGY FILE  4   : WATER.TOP
REMARK   3  TOPOLOGY FILE  5   : ION.TOP
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD
REMARK   4
REMARK   4 1KEQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-01.
REMARK 100 THE RCSB ID CODE IS RCSB014875.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 17-APR-01
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X12B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9796
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL, FIXED-EXIT SI
REMARK 200                                   -III
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46338
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6
REMARK 200  DATA REDUNDANCY                : 3.000
REMARK 200  R MERGE                    (I) : 0.05100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.21700
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.000
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: PDB ENTRY 1DMX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM ACETATE, DTT,
REMARK 280  SUCROSE MONOLAURATE, MES, PH 6.7, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
REMARK 290       4555   -X+1/2,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        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       49.64950
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.35150
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.64950
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.35150
REMARK 290   SMTRY3   4  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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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     CYS A    22
REMARK 465     ALA A    23
REMARK 465     THR A    24
REMARK 465     ASP A   263
REMARK 465     ARG A   264
REMARK 465     THR A   265
REMARK 465     LYS A   266
REMARK 465     MET A   267
REMARK 465     ARG A   268
REMARK 465     SER A   269
REMARK 465     CYS B    22
REMARK 465     ALA B    23
REMARK 465     THR B    24
REMARK 465     ASP B   263
REMARK 465     ARG B   264
REMARK 465     THR B   265
REMARK 465     LYS B   266
REMARK 465     MET B   267
REMARK 465     ARG B   268
REMARK 465     SER B   269
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  57      -52.05   -122.82
REMARK 500    TYR A  64      -32.92   -133.24
REMARK 500    ASP A  72       33.35    -92.06
REMARK 500    ASP A 171       -4.72     70.17
REMARK 500    ASN A 244       57.27    -93.96
REMARK 500    ARG A 252     -135.43     67.02
REMARK 500    ARG B 252     -134.92     67.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     4MZ A  351
REMARK 610     4MZ B  351
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                               K A 305   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 449   O
REMARK 620 2 GLN A 173   OE1  84.3
REMARK 620 3 ASP A 171   O    97.0 100.8
REMARK 620 4 ASP B 171   O   102.9 165.6  90.7
REMARK 620 5 GLN B 173   OE1 156.6  87.4 106.1  81.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 280  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 871   O
REMARK 620 2 HIS A  96   NE2  80.0
REMARK 620 3 HIS A  94   NE2 105.8 101.8
REMARK 620 4 HIS A 119   ND1 136.4  97.9 117.0
REMARK 620 5 ACY A 299   O    88.6 167.9  85.3  87.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 281  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 872   O
REMARK 620 2 ACY B 300   O    81.7
REMARK 620 3 HIS B 119   ND1 136.3  88.0
REMARK 620 4 HIS B  96   NE2  83.4 162.2  96.2
REMARK 620 5 HIS B  94   NE2 105.0  90.8 117.6 102.5
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 305
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 280
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 281
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4MZ A 350
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4MZ A 351
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4MZ A 352
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4MZ B 351
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4MZ B 352
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 299
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 300
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DMX   RELATED DB: PDB
REMARK 900 WT CA-V
DBREF  1KEQ A   22   269  UNP    P23589   CAH5A_MOUSE      1    248
DBREF  1KEQ B   22   269  UNP    P23589   CAH5A_MOUSE      1    248
SEQADV 1KEQ ALA A   65  UNP  P23589    PHE    44 ENGINEERED
SEQADV 1KEQ CYS A  131  UNP  P23589    TYR   110 ENGINEERED
SEQADV 1KEQ ALA B   65  UNP  P23589    PHE    44 ENGINEERED
SEQADV 1KEQ CYS B  131  UNP  P23589    TYR   110 ENGINEERED
SEQRES   1 A  248  CYS ALA THR GLY THR ARG GLN SER PRO ILE ASN ILE GLN
SEQRES   2 A  248  TRP LYS ASP SER VAL TYR ASP PRO GLN LEU ALA PRO LEU
SEQRES   3 A  248  ARG VAL SER TYR ASP ALA ALA SER CYS ARG TYR LEU TRP
SEQRES   4 A  248  ASN THR GLY TYR ALA PHE GLN VAL GLU PHE ASP ASP SER
SEQRES   5 A  248  CYS GLU ASP SER GLY ILE SER GLY GLY PRO LEU GLY ASN
SEQRES   6 A  248  HIS TYR ARG LEU LYS GLN PHE HIS PHE HIS TRP GLY ALA
SEQRES   7 A  248  THR ASP GLU TRP GLY SER GLU HIS ALA VAL ASP GLY HIS
SEQRES   8 A  248  THR TYR PRO ALA GLU LEU HIS LEU VAL HIS TRP ASN SER
SEQRES   9 A  248  THR LYS TYR GLU ASN CYS LYS LYS ALA SER VAL GLY GLU
SEQRES  10 A  248  ASN GLY LEU ALA VAL ILE GLY VAL PHE LEU LYS LEU GLY
SEQRES  11 A  248  ALA HIS HIS GLN ALA LEU GLN LYS LEU VAL ASP VAL LEU
SEQRES  12 A  248  PRO GLU VAL ARG HIS LYS ASP THR GLN VAL ALA MET GLY
SEQRES  13 A  248  PRO PHE ASP PRO SER CYS LEU MET PRO ALA CYS ARG ASP
SEQRES  14 A  248  TYR TRP THR TYR PRO GLY SER LEU THR THR PRO PRO LEU
SEQRES  15 A  248  ALA GLU SER VAL THR TRP ILE VAL GLN LYS THR PRO VAL
SEQRES  16 A  248  GLU VAL SER PRO SER GLN LEU SER MET PHE ARG THR LEU
SEQRES  17 A  248  LEU PHE SER GLY ARG GLY GLU GLU GLU ASP VAL MET VAL
SEQRES  18 A  248  ASN ASN TYR ARG PRO LEU GLN PRO LEU ARG ASP ARG LYS
SEQRES  19 A  248  LEU ARG SER SER PHE ARG LEU ASP ARG THR LYS MET ARG
SEQRES  20 A  248  SER
SEQRES   1 B  248  CYS ALA THR GLY THR ARG GLN SER PRO ILE ASN ILE GLN
SEQRES   2 B  248  TRP LYS ASP SER VAL TYR ASP PRO GLN LEU ALA PRO LEU
SEQRES   3 B  248  ARG VAL SER TYR ASP ALA ALA SER CYS ARG TYR LEU TRP
SEQRES   4 B  248  ASN THR GLY TYR ALA PHE GLN VAL GLU PHE ASP ASP SER
SEQRES   5 B  248  CYS GLU ASP SER GLY ILE SER GLY GLY PRO LEU GLY ASN
SEQRES   6 B  248  HIS TYR ARG LEU LYS GLN PHE HIS PHE HIS TRP GLY ALA
SEQRES   7 B  248  THR ASP GLU TRP GLY SER GLU HIS ALA VAL ASP GLY HIS
SEQRES   8 B  248  THR TYR PRO ALA GLU LEU HIS LEU VAL HIS TRP ASN SER
SEQRES   9 B  248  THR LYS TYR GLU ASN CYS LYS LYS ALA SER VAL GLY GLU
SEQRES  10 B  248  ASN GLY LEU ALA VAL ILE GLY VAL PHE LEU LYS LEU GLY
SEQRES  11 B  248  ALA HIS HIS GLN ALA LEU GLN LYS LEU VAL ASP VAL LEU
SEQRES  12 B  248  PRO GLU VAL ARG HIS LYS ASP THR GLN VAL ALA MET GLY
SEQRES  13 B  248  PRO PHE ASP PRO SER CYS LEU MET PRO ALA CYS ARG ASP
SEQRES  14 B  248  TYR TRP THR TYR PRO GLY SER LEU THR THR PRO PRO LEU
SEQRES  15 B  248  ALA GLU SER VAL THR TRP ILE VAL GLN LYS THR PRO VAL
SEQRES  16 B  248  GLU VAL SER PRO SER GLN LEU SER MET PHE ARG THR LEU
SEQRES  17 B  248  LEU PHE SER GLY ARG GLY GLU GLU GLU ASP VAL MET VAL
SEQRES  18 B  248  ASN ASN TYR ARG PRO LEU GLN PRO LEU ARG ASP ARG LYS
SEQRES  19 B  248  LEU ARG SER SER PHE ARG LEU ASP ARG THR LYS MET ARG
SEQRES  20 B  248  SER
HET      K  A 305       1
HET     ZN  A 280       1
HET     ZN  B 281       1
HET    4MZ  A 350      12
HET    4MZ  A 351       1
HET    4MZ  A 352       6
HET    4MZ  B 351       1
HET    4MZ  B 352       6
HET    ACY  A 299       4
HET    ACY  B 300       4
HET    ACY  A 301       4
HETNAM       K POTASSIUM ION
HETNAM      ZN ZINC ION
HETNAM     4MZ 4-METHYLIMIDAZOLE
HETNAM     ACY ACETIC ACID
FORMUL   3    K    K 1+
FORMUL   4   ZN    2(ZN 2+)
FORMUL   6  4MZ    5(C4 H6 N2)
FORMUL  11  ACY    3(C2 H4 O2)
FORMUL  14  HOH   *471(H2 O)
HELIX    1   1 GLN A   34  LYS A   36  5                                   3
HELIX    2   2 ASP A   52  ALA A   54  5                                   3
HELIX    3   3 ASN A  130  SER A  135  1                                   6
HELIX    4   4 HIS A  154  ASP A  162  1                                   9
HELIX    5   5 VAL A  163  VAL A  167  5                                   5
HELIX    6   6 ASP A  180  MET A  185  5                                   6
HELIX    7   7 SER A  219  ARG A  227  1                                   9
HELIX    8   8 GLN B   34  LYS B   36  5                                   3
HELIX    9   9 ASP B   52  ALA B   54  5                                   3
HELIX   10  10 ASN B  130  SER B  135  1                                   6
HELIX   11  11 HIS B  154  ASP B  162  1                                   9
HELIX   12  12 VAL B  163  ARG B  168  5                                   6
HELIX   13  13 ASP B  180  MET B  185  5                                   6
HELIX   14  14 SER B  219  ARG B  227  1                                   9
SHEET    1  A1 2 ASN A  32  ILE A  33  0
SHEET    2  A1 2 ALA A 108  VAL A 109  1  O  ALA A 108   N  ILE A  33
SHEET    1  A216 GLN A 173  ALA A 175  0
SHEET    2  A216 CYS A  56  ASN A  61 -1  N  LEU A  59   O  VAL A 174
SHEET    3  A216 PHE A  66  PHE A  70 -1  N  GLN A  67   O  TRP A  60
SHEET    4  A216 TYR A  88  TRP A  97 -1  O  LYS A  91   N  PHE A  70
SHEET    5  A216 GLY A  78  GLY A  82 -1  O  ILE A  79   N  TYR A  88
SHEET    6  A216 ALA A  45  SER A  50 -1  N  ALA A  45   O  GLY A  82
SHEET    7  A216 GLY A  78  GLY A  82 -1  O  GLY A  78   N  SER A  50
SHEET    8  A216 TYR A  88  TRP A  97 -1  N  TYR A  88   O  ILE A  79
SHEET    9  A216 ALA A 116  ASN A 124 -1  N  GLU A 117   O  HIS A  96
SHEET   10  A216 LEU A 141  LEU A 150 -1  N  ALA A 142   O  HIS A 122
SHEET   11  A216 VAL A 216  VAL A 218  1  N  VAL A 216   O  PHE A 147
SHEET   12  A216 LEU A 141  LEU A 150  1  O  PHE A 147   N  VAL A 216
SHEET   13  A216 VAL A 207  GLN A 212  1  N  THR A 208   O  LEU A 141
SHEET   14  A216 TYR A 191  GLY A 196 -1  O  TRP A 192   N  VAL A 211
SHEET   15  A216 LEU A 256  SER A 258 -1  O  ARG A 257   N  THR A 193
SHEET   16  A216 SER A  38  TYR A  40  1  O  VAL A  39   N  SER A 258
SHEET    1  B1 2 ASN B  32  ILE B  33  0
SHEET    2  B1 2 ALA B 108  VAL B 109  1  O  ALA B 108   N  ILE B  33
SHEET    1  B216 GLN B 173  ALA B 175  0
SHEET    2  B216 CYS B  56  ASN B  61 -1  N  LEU B  59   O  VAL B 174
SHEET    3  B216 PHE B  66  PHE B  70 -1  N  GLN B  67   O  TRP B  60
SHEET    4  B216 TYR B  88  TRP B  97 -1  O  LYS B  91   N  PHE B  70
SHEET    5  B216 GLY B  78  GLY B  82 -1  O  ILE B  79   N  TYR B  88
SHEET    6  B216 ALA B  45  SER B  50 -1  N  ALA B  45   O  GLY B  82
SHEET    7  B216 GLY B  78  GLY B  82 -1  O  GLY B  78   N  SER B  50
SHEET    8  B216 TYR B  88  TRP B  97 -1  N  TYR B  88   O  ILE B  79
SHEET    9  B216 ALA B 116  ASN B 124 -1  N  GLU B 117   O  HIS B  96
SHEET   10  B216 LEU B 141  LEU B 150 -1  N  ALA B 142   O  HIS B 122
SHEET   11  B216 VAL B 216  VAL B 218  1  N  VAL B 216   O  PHE B 147
SHEET   12  B216 LEU B 141  LEU B 150  1  O  PHE B 147   N  VAL B 216
SHEET   13  B216 VAL B 207  GLN B 212  1  N  THR B 208   O  LEU B 141
SHEET   14  B216 TYR B 191  GLY B 196 -1  O  TRP B 192   N  VAL B 211
SHEET   15  B216 LEU B 256  SER B 258 -1  O  ARG B 257   N  THR B 193
SHEET   16  B216 SER B  38  TYR B  40  1  O  VAL B  39   N  SER B 258
LINK         SG  CYS A 183                 C4  4MZ A 351     1555   1555  1.78
LINK         SG  CYS B 183                 C4  4MZ B 351     1555   1555  1.79
LINK         SG  CYS A 188                 C4  4MZ A 352     1555   1555  1.82
LINK         SG  CYS B 188                 C4  4MZ B 352     1555   1555  1.82
LINK         SG  CYS A 131                 C4 A4MZ A 350     1555   1555  1.82
LINK         SG  CYS A 131                 C4 B4MZ A 350     1555   1555  1.82
LINK         K     K A 305                 O   HOH A 449     1555   1555  2.33
LINK        ZN    ZN A 280                 O   HOH A 871     1555   1555  1.93
LINK        ZN    ZN B 281                 O   HOH B 872     1555   1555  1.91
LINK        ZN    ZN A 280                 NE2 HIS A  96     1555   1555  2.19
LINK        ZN    ZN A 280                 NE2 HIS A  94     1555   1555  2.01
LINK        ZN    ZN A 280                 ND1 HIS A 119     1555   1555  2.04
LINK        ZN    ZN A 280                 O   ACY A 299     1555   1555  2.45
LINK         K     K A 305                 OE1 GLN A 173     1555   1555  2.33
LINK         K     K A 305                 O   ASP A 171     1555   1555  2.27
LINK        ZN    ZN B 281                 O   ACY B 300     1555   1555  2.39
LINK        ZN    ZN B 281                 ND1 HIS B 119     1555   1555  2.03
LINK        ZN    ZN B 281                 NE2 HIS B  96     1555   1555  2.11
LINK        ZN    ZN B 281                 NE2 HIS B  94     1555   1555  1.97
LINK         K     K A 305                 O   ASP B 171     1555   3445  2.42
LINK         K     K A 305                 OE1 GLN B 173     1555   3445  2.38
CISPEP   1 SER A   29    PRO A   30          0         0.05
CISPEP   2 PRO A  201    PRO A  202          0         0.11
CISPEP   3 SER B   29    PRO B   30          0         0.03
CISPEP   4 PRO B  201    PRO B  202          0         0.10
SITE     1 AC1  5 ASP A 171  GLN A 173  HOH A 449  ASP B 171
SITE     2 AC1  5 GLN B 173
SITE     1 AC2  5 HIS A  94  HIS A  96  HIS A 119  ACY A 299
SITE     2 AC2  5 HOH A 871
SITE     1 AC3  5 HIS B  94  HIS B  96  HIS B 119  ACY B 300
SITE     2 AC3  5 HOH B 872
SITE     1 AC4  4 GLN A  92  CYS A 131  SER A 135  HOH A 577
SITE     1 AC5  1 CYS A 183
SITE     1 AC6  2 CYS A 188  ASP A 190
SITE     1 AC7  1 CYS B 183
SITE     1 AC8  2 CYS B 188  ASP B 190
SITE     1 AC9  6 HIS A  94  HIS A 119  LEU A 198  THR A 199
SITE     2 AC9  6  ZN A 280  HOH A 871
SITE     1 BC1  7 HIS B  94  HIS B 119  LEU B 198  THR B 199
SITE     2 BC1  7 TRP B 209   ZN B 281  HOH B 872
SITE     1 BC2  6 LEU A  47  VAL A  49  ARG A 189  HOH A 498
SITE     2 BC2  6 HOH A 558  HOH A 696
CRYST1   99.299   66.703   92.563  90.00 105.70  90.00 C 1 2 1       8
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      0.010071  0.000000  0.002831        0.00000
SCALE2      0.000000  0.014992  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011222        0.00000
      
PROCHECK
Go to PROCHECK summary
 References