spacer
spacer

PDBsum entry 3m2y

Go to PDB code: 
Top Page protein ligands metals links
Lyase/lyase inhibitor PDB id
3m2y
Jmol
Contents
Protein chain
258 a.a.
Ligands
BE0 ×2
BE7
Metals
_ZN ×2
_HG
Waters ×266
HEADER    LYASE/LYASE INHIBITOR                   08-MAR-10   3M2Y
TITLE     CARBONIC ANHYDRASE II IN COMPLEX WITH NOVEL SULFONAMIDE INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: CARBONIC ANHYDRASE II;
COMPND   5 SYNONYM: CARBONIC ANHYDRASE II, CA-II, CARBONATE DEHYDRATASE II,
COMPND   6 CARBONIC ANHYDRASE C, CAC;
COMPND   7 EC: 4.2.1.1;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CA2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 CODON PLUS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T1
KEYWDS    10 STRANDED TWISTED BETA-SHEETS, LYASE, DISEASE MUTATION, METAL-
KEYWDS   2 BINDING, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.SCHULZE WISCHELER,A.HEINE,G.KLEBE
REVDAT   1   25-MAY-11 3M2Y    0
JRNL        AUTH   J.SCHULZE WISCHELER,N.U.SANDNER,M.HAAKE,C.SUPURAN,A.HEINE,
JRNL        AUTH 2 G.KLEBE
JRNL        TITL   STRUCTURAL INVESTIGATION AND INHIBITOR STUIES ON CARBONIC
JRNL        TITL 2 ANHYDRASE II
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.17 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) : 1.17
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3
REMARK   3   CROSS-VALIDATION METHOD           : FREE R
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) : 0.128
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.127
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.161
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 3947
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 77967
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.124
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)) : 70416
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2043
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 32
REMARK   3   SOLVENT ATOMS      : 266
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2339.48
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1975.86
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 7
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 21322
REMARK   3   NUMBER OF RESTRAINTS                     : 26593
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.021
REMARK   3   ANGLE DISTANCES                      (A) : 0.030
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.031
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.077
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.081
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.068
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.041
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.080
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK   3  METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
REMARK   3  ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY ?
REMARK   4
REMARK   4 3M2Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-10.
REMARK 100 THE RCSB ID CODE IS RCSB058041.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 110
REMARK 200  PH                             : 7.8
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) : 0.91841
REMARK 200  MONOCHROMATOR                  : SI-111 CRYSTAL
REMARK 200  OPTICS                         : SILICON
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79675
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.170
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3
REMARK 200  DATA REDUNDANCY                : 3.000
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.04800
REMARK 200   FOR THE DATA SET  : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.17
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.19
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.18200
REMARK 200   FOR SHELL         : 5.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1OQ5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M AMMONIUM SULFATE  50 MM TRIS
REMARK 280  0.1 MM P-CHLOROMERCURIBENZOIC ACID 1 MM SULFONAMIDE, PH 7.8,
REMARK 280  VAPOR DIFFUSION, SITTING 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       20.70000
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     GLY A    -4
REMARK 465     SER A    -3
REMARK 465     PRO A    -2
REMARK 465     GLU A    -1
REMARK 465     PHE A     0
REMARK 465     MET A     1
REMARK 465     LYS A   261
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 A   9    CG   CD   CE   NZ
REMARK 470     LYS A  45    CG   CD   CE   NZ
REMARK 470     LYS A  76    CG   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    HIS A  96   CG    HIS A  96   CD2     0.058
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    HIS A  15   CG  -  ND1 -  CE1 ANGL. DEV. =  10.6 DEGREES
REMARK 500    HIS A  15   ND1 -  CE1 -  NE2 ANGL. DEV. =  -8.1 DEGREES
REMARK 500    ARG A  27   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES
REMARK 500    ARG A  27   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES
REMARK 500    ARG A  27   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES
REMARK 500    TYR A  51   CB  -  CG  -  CD1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ASP A 130   OD1 -  CG  -  OD2 ANGL. DEV. = -14.0 DEGREES
REMARK 500    ASP A 130   CB  -  CG  -  OD1 ANGL. DEV. =   8.6 DEGREES
REMARK 500    ASP A 175   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG A 182   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG A 227   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 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 A  11       17.63   -142.24
REMARK 500    ARG A  27       53.02   -141.42
REMARK 500    GLU A 106      -62.43    -91.53
REMARK 500    LYS A 111       -3.04     74.73
REMARK 500    PHE A 176       61.28   -150.40
REMARK 500    ASN A 244       47.88    -94.42
REMARK 500    LYS A 252     -138.67     54.50
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 A1196        DISTANCE =  6.04 ANGSTROMS
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     BE7 A  505
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 500  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 BE0 A 504   N2
REMARK 620 2 HIS A  94   NE2 107.3
REMARK 620 3 HIS A  96   NE2 116.1 104.0
REMARK 620 4 HIS A 119   ND1 115.6 114.9  98.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              HG A 501  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1171   O
REMARK 620 2 GLN A 137   O   133.1
REMARK 620 3 GLU A 205   O   132.6  93.0
REMARK 620 N                    1     2
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BE0 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BE0 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BE7 A 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KIG   RELATED DB: PDB
REMARK 900 RELATED ID: 3KNE   RELATED DB: PDB
REMARK 900 RELATED ID: 2Q38   RELATED DB: PDB
REMARK 900 RELATED ID: 3M04   RELATED DB: PDB
REMARK 900 RELATED ID: 3M14   RELATED DB: PDB
REMARK 900 RELATED ID: 3M1K   RELATED DB: PDB
REMARK 900 RELATED ID: 3M1Q   RELATED DB: PDB
REMARK 900 RELATED ID: 3M1W   RELATED DB: PDB
REMARK 900 RELATED ID: 3M2X   RELATED DB: PDB
REMARK 900 RELATED ID: 3M2Z   RELATED DB: PDB
DBREF  3M2Y A    1   261  UNP    P00918   CAH2_HUMAN       1    260
SEQADV 3M2Y GLY A   -4  UNP  P00918              EXPRESSION TAG
SEQADV 3M2Y SER A   -3  UNP  P00918              EXPRESSION TAG
SEQADV 3M2Y PRO A   -2  UNP  P00918              EXPRESSION TAG
SEQADV 3M2Y GLU A   -1  UNP  P00918              EXPRESSION TAG
SEQADV 3M2Y PHE A    0  UNP  P00918              EXPRESSION TAG
SEQRES   1 A  265  GLY SER PRO GLU PHE MET SER HIS HIS TRP GLY TYR GLY
SEQRES   2 A  265  LYS HIS ASN GLY PRO GLU HIS TRP HIS LYS ASP PHE PRO
SEQRES   3 A  265  ILE ALA LYS GLY GLU ARG GLN SER PRO VAL ASP ILE ASP
SEQRES   4 A  265  THR HIS THR ALA LYS TYR ASP PRO SER LEU LYS PRO LEU
SEQRES   5 A  265  SER VAL SER TYR ASP GLN ALA THR SER LEU ARG ILE LEU
SEQRES   6 A  265  ASN ASN GLY HIS ALA PHE ASN VAL GLU PHE ASP ASP SER
SEQRES   7 A  265  GLN ASP LYS ALA VAL LEU LYS GLY GLY PRO LEU ASP GLY
SEQRES   8 A  265  THR TYR ARG LEU ILE GLN PHE HIS PHE HIS TRP GLY SER
SEQRES   9 A  265  LEU ASP GLY GLN GLY SER GLU HIS THR VAL ASP LYS LYS
SEQRES  10 A  265  LYS TYR ALA ALA GLU LEU HIS LEU VAL HIS TRP ASN THR
SEQRES  11 A  265  LYS TYR GLY ASP PHE GLY LYS ALA VAL GLN GLN PRO ASP
SEQRES  12 A  265  GLY LEU ALA VAL LEU GLY ILE PHE LEU LYS VAL GLY SER
SEQRES  13 A  265  ALA LYS PRO GLY LEU GLN LYS VAL VAL ASP VAL LEU ASP
SEQRES  14 A  265  SER ILE LYS THR LYS GLY LYS SER ALA ASP PHE THR ASN
SEQRES  15 A  265  PHE ASP PRO ARG GLY LEU LEU PRO GLU SER LEU ASP TYR
SEQRES  16 A  265  TRP THR TYR PRO GLY SER LEU THR THR PRO PRO LEU LEU
SEQRES  17 A  265  GLU CYS VAL THR TRP ILE VAL LEU LYS GLU PRO ILE SER
SEQRES  18 A  265  VAL SER SER GLU GLN VAL LEU LYS PHE ARG LYS LEU ASN
SEQRES  19 A  265  PHE ASN GLY GLU GLY GLU PRO GLU GLU LEU MET VAL ASP
SEQRES  20 A  265  ASN TRP ARG PRO ALA GLN PRO LEU LYS ASN ARG GLN ILE
SEQRES  21 A  265  LYS ALA SER PHE LYS
HET     ZN  A 500       1
HET     HG  A 501       1
HET     ZN  A 502       1
HET    BE0  A 503      10
HET    BE0  A 504      10
HET    BE7  A 505       9
HETNAM      ZN ZINC ION
HETNAM      HG MERCURY (II) ION
HETNAM     BE0 PIPERIDINE-1-SULFONAMIDE
HETNAM     BE7 (4-CARBOXYPHENYL)(CHLORO)MERCURY
HETSYN     BE7 P-CHLOROMERCURIBENZOIC ACID
FORMUL   2   ZN    2(ZN 2+)
FORMUL   3   HG    HG 2+
FORMUL   5  BE0    2(C5 H12 N2 O2 S)
FORMUL   7  BE7    C7 H5 CL HG O2
FORMUL   8  HOH   *266(H2 O)
HELIX    1   1 HIS A   15  ASP A   19  5                                   5
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A  127  GLY A  129  5                                   3
HELIX    4   4 ASP A  130  VAL A  135  1                                   6
HELIX    5   5 LYS A  154  GLY A  156  5                                   3
HELIX    6   6 LEU A  157  LEU A  164  1                                   8
HELIX    7   7 ASP A  165  LYS A  168  5                                   4
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  ARG A  227  1                                   9
SHEET    1   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   B10 LYS A  39  TYR A  40  0
SHEET    2   B10 LYS A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4   B10 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B10 LEU A 141  VAL A 150  1  N  GLY A 145   O  LEU A 212
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 146
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  HIS A  94   O  HIS A 119
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9   B10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   10   B10 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 LEU A  47  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  81 -1  O  VAL A  78   N  SER A  50
SHEET    3   C 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET    4   C 6 ALA A 116  ASN A 124 -1  O  HIS A 119   N  HIS A  94
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ILE A 146   N  LEU A 118
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  PHE A 147
LINK        ZN    ZN A 500                 N2  BE0 A 504     1555   1555  1.96
LINK         NE2 HIS A  94                ZN    ZN A 500     1555   1555  1.99
LINK         NE2 HIS A  96                ZN    ZN A 500     1555   1555  2.01
LINK         ND1 HIS A 119                ZN    ZN A 500     1555   1555  2.04
LINK         ND1 HIS A  64                ZN    ZN A 502     1555   1555  2.49
LINK        HG    HG A 501                 O   HOH A1171     1555   1555  2.96
LINK         O   GLN A 137                HG    HG A 501     1555   1555  2.96
LINK         O   GLU A 205                HG    HG A 501     1555   1555  3.02
CISPEP   1 SER A   29    PRO A   30          0        -1.44
CISPEP   2 PRO A  201    PRO A  202          0        12.61
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  BE0 A 504
SITE     1 AC2  5 GLN A 137  GLU A 205  CYS A 206  BE7 A 505
SITE     2 AC2  5 HOH A1171
SITE     1 AC3  3 ASN A  62  GLY A  63  HIS A  64
SITE     1 AC4  8 HIS A   3  TRP A   5  HIS A  10  HIS A  15
SITE     2 AC4  8 TRP A  16  ASP A  19  PHE A  20  HOH A1200
SITE     1 AC5  9 HIS A  94  HIS A  96  HIS A 119  VAL A 121
SITE     2 AC5  9 LEU A 198  THR A 199  THR A 200  TRP A 209
SITE     3 AC5  9  ZN A 500
SITE     1 AC6  4 GLN A 136  PRO A 138  GLU A 205   HG A 501
CRYST1   42.400   41.400   72.200  90.00 104.60  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      0.023585  0.000000  0.006143        0.00000
SCALE2      0.000000  0.024155  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014313        0.00000
      
PROCHECK
Go to PROCHECK summary
 References