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PDBsum entry 3ucn

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase/lyase inhibitor PDB id
3ucn
Jmol
Contents
Protein chains
222 a.a.
Ligands
AZI ×2
Metals
_CL
_ZN ×2
Waters ×189
HEADER    LYASE/LYASE INHIBITOR                   27-OCT-11   3UCN
TITLE     COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH AZIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 4.2.1.1;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: COCCOMYXA SP. PA;
SOURCE   3 ORGANISM_TAXID: 41892;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PMAL-C2
KEYWDS    ALPHA/BETA, STRAND EXCHANGE, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.HUANG,T.HAINZL,A.E.SAUER-ERIKSSON
REVDAT   2   28-MAR-12 3UCN    1       JRNL
REVDAT   1   23-NOV-11 3UCN    0
JRNL        AUTH   S.HUANG,T.HAINZL,C.GRUNDSTROM,C.FORSMAN,G.SAMUELSSON,
JRNL        AUTH 2 A.E.SAUER-ERIKSSON
JRNL        TITL   STRUCTURAL STUDIES OF [BETA]-CARBONIC ANHYDRASE FROM THE
JRNL        TITL 2 GREEN ALGA COCCOMYXA: INHIBITOR COMPLEXES WITH ANIONS AND
JRNL        TITL 3 ACETAZOLAMIDE.
JRNL        REF    PLOS ONE                      V.   6 28458 2011
JRNL        REFN                   ESSN 1932-6203
JRNL        PMID   22162771
JRNL        DOI    10.1371/JOURNAL.PONE.0028458
REMARK   2
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0110
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) : 2.25
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.32
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7
REMARK   3   NUMBER OF REFLECTIONS             : 29338
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) : 0.161
REMARK   3   R VALUE            (WORKING SET) : 0.159
REMARK   3   FREE R VALUE                     : 0.200
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1561
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) : 2.25
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2125
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.99
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2700
REMARK   3   BIN FREE R VALUE SET COUNT          : 112
REMARK   3   BIN FREE R VALUE                    : 0.3050
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3390
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 9
REMARK   3   SOLVENT ATOMS            : 189
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.14
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.22000
REMARK   3    B22 (A**2) : 0.22000
REMARK   3    B33 (A**2) : -0.44000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.179
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.161
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.833
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3468 ; 0.023 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4710 ; 1.909 ; 1.948
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   442 ; 6.248 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   146 ;42.421 ;24.795
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   568 ;17.024 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;12.901 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   530 ; 0.131 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2618 ; 0.010 ; 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):  2208 ; 1.149 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3534 ; 2.168 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1260 ; 3.650 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1176 ; 6.131 ; 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   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK   3  U VALUES      : REFINED INDIVIDUALLY
REMARK   4
REMARK   4 3UCN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-11.
REMARK 100 THE RCSB ID CODE IS RCSB068586.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-00
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 7.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR591
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NI FILTER, PT MIRRORS
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAC SCIENCE DIP-2030
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29541
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.317
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07800
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.61800
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 3UCJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6-2.3 M SODIUM/POTASSIUM PHOSPHATE,
REMARK 280  2.5 MM AZIDE, PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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      111.11050
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       37.82550
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       37.82550
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      166.66575
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       37.82550
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       37.82550
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       55.55525
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       37.82550
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       37.82550
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      166.66575
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       37.82550
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       37.82550
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       55.55525
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      111.11050
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -306.0 KCAL/MOL
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 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      222.22100
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     ALA A     3
REMARK 465     LYS A     4
REMARK 465     ASP A     5
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     ALA B     3
REMARK 465     LYS B     4
REMARK 465     ASP B     5
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    ASP A  49      124.71    -33.64
REMARK 500    SER A  50       -9.72    -57.44
REMARK 500    LYS A 200      159.77    -49.36
REMARK 500    ASP B  49      127.33    -37.08
REMARK 500    ALA B 146      -58.79    -28.76
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 228  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 AZI A 229   N1
REMARK 620 2 HIS A 103   NE2 113.7
REMARK 620 3 CYS A  47   SG   98.7 113.5
REMARK 620 4 CYS A 106   SG  105.8 101.4 124.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 228  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 AZI A 230   N1
REMARK 620 2 HIS B 103   NE2 118.6
REMARK 620 3 CYS B 106   SG   98.8 105.1
REMARK 620 4 CYS B  47   SG  104.1 108.9 121.9
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 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI A 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI A 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 231
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UCJ   RELATED DB: PDB
REMARK 900 COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH
REMARK 900 ACETAZOLAMIDE
REMARK 900 RELATED ID: 3UCK   RELATED DB: PDB
REMARK 900 COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH PHOSPHATE
REMARK 900 RELATED ID: 3UCM   RELATED DB: PDB
REMARK 900 COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH
REMARK 900 THIOCYANATE
REMARK 900 RELATED ID: 3UCO   RELATED DB: PDB
REMARK 900 COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH IODIDE
DBREF  3UCN A    1   227  UNP    Q96554   Q96554_9CHLO     1    227
DBREF  3UCN B    1   227  UNP    Q96554   Q96554_9CHLO     1    227
SEQRES   1 A  227  MET SER ALA LYS ASP THR ALA ASP LEU SER PRO LEU LEU
SEQRES   2 A  227  GLU ALA ASN ARG LYS TRP ALA ASP GLU CYS ALA ALA LYS
SEQRES   3 A  227  ASP SER THR TYR PHE SER LYS VAL ALA GLY SER GLN ALA
SEQRES   4 A  227  PRO GLU TYR LEU TYR ILE GLY CYS ALA ASP SER ARG VAL
SEQRES   5 A  227  SER PRO ALA GLN LEU PHE ASN MET ALA PRO GLY GLU VAL
SEQRES   6 A  227  PHE VAL GLN ARG ASN VAL GLY ASN LEU VAL SER ASN LYS
SEQRES   7 A  227  ASP LEU ASN CYS MET SER CYS LEU GLU TYR THR VAL ASP
SEQRES   8 A  227  HIS LEU LYS ILE LYS HIS ILE LEU VAL CYS GLY HIS TYR
SEQRES   9 A  227  ASN CYS GLY ALA CYS LYS ALA GLY LEU VAL TRP HIS PRO
SEQRES  10 A  227  LYS THR ALA GLY VAL THR ASN LEU TRP ILE SER ASP VAL
SEQRES  11 A  227  ARG GLU VAL ARG ASP LYS ASN ALA ALA LYS LEU HIS GLY
SEQRES  12 A  227  LEU SER ALA ASP ASP ALA TRP ASP LYS MET VAL GLU LEU
SEQRES  13 A  227  ASN VAL GLU ALA GLN VAL PHE ASN VAL CYS ALA SER PRO
SEQRES  14 A  227  ILE VAL GLN ALA ALA TRP ALA ARG GLY GLN PRO LEU SER
SEQRES  15 A  227  VAL HIS GLY ILE VAL TYR THR PRO GLY THR GLY LEU VAL
SEQRES  16 A  227  LYS GLU LEU ILE LYS PRO ILE THR GLY MET GLU ASP ALA
SEQRES  17 A  227  GLY ALA LEU LEU ARG ALA ASP LEU LYS GLN HIS CYS PHE
SEQRES  18 A  227  PHE SER GLU SER LEU ALA
SEQRES   1 B  227  MET SER ALA LYS ASP THR ALA ASP LEU SER PRO LEU LEU
SEQRES   2 B  227  GLU ALA ASN ARG LYS TRP ALA ASP GLU CYS ALA ALA LYS
SEQRES   3 B  227  ASP SER THR TYR PHE SER LYS VAL ALA GLY SER GLN ALA
SEQRES   4 B  227  PRO GLU TYR LEU TYR ILE GLY CYS ALA ASP SER ARG VAL
SEQRES   5 B  227  SER PRO ALA GLN LEU PHE ASN MET ALA PRO GLY GLU VAL
SEQRES   6 B  227  PHE VAL GLN ARG ASN VAL GLY ASN LEU VAL SER ASN LYS
SEQRES   7 B  227  ASP LEU ASN CYS MET SER CYS LEU GLU TYR THR VAL ASP
SEQRES   8 B  227  HIS LEU LYS ILE LYS HIS ILE LEU VAL CYS GLY HIS TYR
SEQRES   9 B  227  ASN CYS GLY ALA CYS LYS ALA GLY LEU VAL TRP HIS PRO
SEQRES  10 B  227  LYS THR ALA GLY VAL THR ASN LEU TRP ILE SER ASP VAL
SEQRES  11 B  227  ARG GLU VAL ARG ASP LYS ASN ALA ALA LYS LEU HIS GLY
SEQRES  12 B  227  LEU SER ALA ASP ASP ALA TRP ASP LYS MET VAL GLU LEU
SEQRES  13 B  227  ASN VAL GLU ALA GLN VAL PHE ASN VAL CYS ALA SER PRO
SEQRES  14 B  227  ILE VAL GLN ALA ALA TRP ALA ARG GLY GLN PRO LEU SER
SEQRES  15 B  227  VAL HIS GLY ILE VAL TYR THR PRO GLY THR GLY LEU VAL
SEQRES  16 B  227  LYS GLU LEU ILE LYS PRO ILE THR GLY MET GLU ASP ALA
SEQRES  17 B  227  GLY ALA LEU LEU ARG ALA ASP LEU LYS GLN HIS CYS PHE
SEQRES  18 B  227  PHE SER GLU SER LEU ALA
HET     ZN  A 228       1
HET    AZI  A 229       3
HET    AZI  A 230       3
HET     CL  A 231       1
HET     ZN  B 228       1
HETNAM      ZN ZINC ION
HETNAM     AZI AZIDE ION
HETNAM      CL CHLORIDE ION
FORMUL   3   ZN    2(ZN 2+)
FORMUL   4  AZI    2(N3 1-)
FORMUL   6   CL    CL 1-
FORMUL   8  HOH   *189(H2 O)
HELIX    1   1 LEU A    9  ASP A   27  1                                  19
HELIX    2   2 PHE A   31  ALA A   35  5                                   5
HELIX    3   3 SER A   53  PHE A   58  1                                   6
HELIX    4   4 ASP A   79  HIS A   92  1                                  14
HELIX    5   5 CYS A  106  TRP A  115  1                                  10
HELIX    6   6 GLY A  121  ILE A  127  1                                   7
HELIX    7   7 ILE A  127  ASN A  137  1                                  11
HELIX    8   8 ASN A  137  HIS A  142  1                                   6
HELIX    9   9 SER A  145  SER A  168  1                                  24
HELIX   10  10 SER A  168  ARG A  177  1                                  10
HELIX   11  11 GLY A  204  LEU A  212  1                                   9
HELIX   12  12 ASP A  215  PHE A  221  1                                   7
HELIX   13  13 PHE A  222  LEU A  226  5                                   5
HELIX   14  14 LEU B    9  ASP B   27  1                                  19
HELIX   15  15 PHE B   31  ALA B   35  5                                   5
HELIX   16  16 SER B   53  PHE B   58  1                                   6
HELIX   17  17 ASP B   79  HIS B   92  1                                  14
HELIX   18  18 CYS B  106  TRP B  115  1                                  10
HELIX   19  19 GLY B  121  ILE B  127  1                                   7
HELIX   20  20 ILE B  127  ASN B  137  1                                  11
HELIX   21  21 ALA B  138  LEU B  141  5                                   4
HELIX   22  22 SER B  145  ALA B  167  1                                  23
HELIX   23  23 SER B  168  ARG B  177  1                                  10
HELIX   24  24 GLY B  204  LEU B  212  1                                   9
HELIX   25  25 ASP B  215  PHE B  222  1                                   8
HELIX   26  26 SER B  223  LEU B  226  5                                   4
SHEET    1   A 5 VAL A  65  ASN A  70  0
SHEET    2   A 5 TYR A  42  CYS A  47  1  N  TYR A  42   O  PHE A  66
SHEET    3   A 5 HIS A  97  HIS A 103  1  O  LEU A  99   N  ILE A  45
SHEET    4   A 5 SER A 182  TYR A 188  1  O  SER A 182   N  ILE A  98
SHEET    5   A 5 VAL A 195  ILE A 202 -1  O  ILE A 202   N  VAL A 183
SHEET    1   B 5 VAL B  65  ASN B  70  0
SHEET    2   B 5 TYR B  42  CYS B  47  1  N  TYR B  44   O  GLN B  68
SHEET    3   B 5 HIS B  97  HIS B 103  1  O  LEU B  99   N  LEU B  43
SHEET    4   B 5 SER B 182  TYR B 188  1  O  ILE B 186   N  VAL B 100
SHEET    5   B 5 VAL B 195  ILE B 202 -1  O  LEU B 198   N  GLY B 185
LINK        ZN    ZN A 228                 N1  AZI A 229     1555   1555  1.85
LINK        ZN    ZN B 228                 N1  AZI A 230     1555   1555  2.11
LINK         NE2 HIS B 103                ZN    ZN B 228     1555   1555  2.13
LINK         NE2 HIS A 103                ZN    ZN A 228     1555   1555  2.17
LINK         SG  CYS B 106                ZN    ZN B 228     1555   1555  2.30
LINK         SG  CYS A  47                ZN    ZN A 228     1555   1555  2.31
LINK         SG  CYS B  47                ZN    ZN B 228     1555   1555  2.33
LINK         SG  CYS A 106                ZN    ZN A 228     1555   1555  2.36
SITE     1 AC1  4 CYS A  47  HIS A 103  CYS A 106  AZI A 229
SITE     1 AC2  4 AZI A 230  CYS B  47  HIS B 103  CYS B 106
SITE     1 AC3  9 CYS A  47  ASP A  49  HIS A 103  CYS A 106
SITE     2 AC3  9 GLY A 107   ZN A 228  GLN B  38  PHE B  66
SITE     3 AC3  9 TYR B  88
SITE     1 AC4  9 GLN A  38  PHE A  66  CYS B  47  ASP B  49
SITE     2 AC4  9 HIS B 103  CYS B 106  GLY B 107  ALA B 108
SITE     3 AC4  9  ZN B 228
SITE     1 AC5  4 ARG A  69  HOH A 318  ARG B  69  HOH B 329
CRYST1   75.651   75.651  222.221  90.00  90.00  90.00 P 43 21 2    16
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      0.013219  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013219  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004500        0.00000
      
PROCHECK
Go to PROCHECK summary
 References