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PDBsum entry 2zvj

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Transferase PDB id
2zvj
Jmol
Contents
Protein chain
212 a.a.
Ligands
SAM
KOM
Metals
_MG
Waters ×73
HEADER    TRANSFERASE                             07-NOV-08   2ZVJ
TITLE     CRYSTAL STRUCTURES OF RAT CATECHOL-O-METHYLTRANSFERASE
TITLE    2 COMPLEXED WITH COUMARINE-BASED INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 44-264;
COMPND   5 EC: 2.1.1.6;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE   3 ORGANISM_COMMON: RAT;
SOURCE   4 ORGANISM_TAXID: 10116;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 CODON PLUS(DE3)RP;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS    TRANSFERASE, METHYLTRANSFERASE, NEUROTRANSMITTER
KEYWDS   2 DEGRADATION, ALTERNATIVE INITIATION, CATECHOLAMINE
KEYWDS   3 METABOLISM, CELL MEMBRANE, CYTOPLASM, MAGNESIUM, MEMBRANE,
KEYWDS   4 METAL-BINDING, PHOSPHOPROTEIN, S-ADENOSYL-L-METHIONINE,
KEYWDS   5 SIGNAL-ANCHOR, TRANSMEMBRANE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.TSUJI
REVDAT   1   06-JAN-09 2ZVJ    0
JRNL        AUTH   E.TSUJI,K.OKAZAKI,K.TAKEDA
JRNL        TITL   CRYSTAL STRUCTURES OF RAT
JRNL        TITL 2 CATECHOL-O-METHYLTRANSFERASE COMPLEXED WITH
JRNL        TITL 3 COUMARINE-BASED INHIBITOR
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 378   494 2009
JRNL        REFN                   ISSN 0006-291X
JRNL        PMID   19056347
JRNL        DOI    10.1016/J.BBRC.2008.11.085
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.30
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6
REMARK   3   NUMBER OF REFLECTIONS             : 10454
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) : 0.219
REMARK   3   R VALUE            (WORKING SET) : 0.211
REMARK   3   FREE R VALUE                     : 0.286
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800
REMARK   3   FREE R VALUE TEST SET COUNT      : 1134
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) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 707
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2730
REMARK   3   BIN FREE R VALUE SET COUNT          : 92
REMARK   3   BIN FREE R VALUE                    : 0.3140
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1672
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 47
REMARK   3   SOLVENT ATOMS            : 73
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 49.50
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.81
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.22000
REMARK   3    B22 (A**2) : 2.22000
REMARK   3    B33 (A**2) : -3.32000
REMARK   3    B12 (A**2) : 1.11000
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): 0.373
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.283
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.208
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.704
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1754 ; 0.015 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2381 ; 1.667 ; 2.017
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   211 ; 5.777 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    76 ;39.270 ;24.868
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   305 ;17.589 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;19.738 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   265 ; 0.112 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1313 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   909 ; 0.230 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1171 ; 0.310 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   114 ; 0.210 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.045 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    20 ; 0.201 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.067 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1091 ; 0.933 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1706 ; 1.564 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   804 ; 1.798 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   675 ; 2.829 ; 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 : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 2ZVJ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-NOV-08.
REMARK 100 THE RCSB ID CODE IS RCSB028478.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL32B2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11591
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.300
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : 6.800
REMARK 200  R MERGE                    (I) : 0.07400
REMARK 200  R SYM                      (I) : 0.06800
REMARK 200   FOR THE DATA SET  : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.18100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 8.200
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 1VID
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M (NH4)2SO4, 30% PEG 8000, 0.1M
REMARK 280  TRIS PH7.5, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+1/3
REMARK 290       6555   -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      111.75067
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       55.87533
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       55.87533
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      111.75067
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    -1
REMARK 465     SER A     0
REMARK 465     MET A     1
REMARK 465     GLY A     2
REMARK 465     PRO A   215
REMARK 465     SER A   216
REMARK 465     SER A   217
REMARK 465     PRO A   218
REMARK 465     ASP A   219
REMARK 465     LYS A   220
REMARK 465     SER A   221
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   SD   MET A    40     O    HOH A   348              2.17
REMARK 500   OE1  GLU A    64     OG   SER A    72              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    LYS A  36      -77.13   -118.25
REMARK 500    MET A  40       34.25    -99.54
REMARK 500    SER A  58       70.34     29.36
REMARK 500    TYR A  68     -115.91     65.85
REMARK 500    ASP A 133      -79.65    -91.16
REMARK 500    ASP A 141       31.31   -151.65
REMARK 500    HIS A 142     -148.89    -94.90
REMARK 500    SER A 196     -152.62   -160.28
REMARK 500    TYR A 200       -0.64     69.52
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                              MG A 300  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141   OD2
REMARK 620 2 ASP A 169   OD2  98.5
REMARK 620 3 ASN A 170   OD1  84.5  94.2
REMARK 620 4 KOM A 302   O9   72.7 165.5  73.8
REMARK 620 5 HOH A 371   O    90.7  95.2 170.0  96.4
REMARK 620 6 KOM A 302   O10 151.6 109.4  98.3  80.9  81.8
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 300
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 301
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KOM A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VID   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATECHOL O-METHYLTRANSFERASE
REMARK 900 RELATED ID: 1H1D   RELATED DB: PDB
REMARK 900 CATECHOL O-METHYLTRANSFERASE
REMARK 900 RELATED ID: 2CL5   RELATED DB: PDB
REMARK 900 CATECHOL-O-METHYLTRANSFERASE IN COMPLEX WITH AN INHIBITOR
REMARK 900 RELATED ID: 1JR4   RELATED DB: PDB
REMARK 900 CATECHOL O-METHYLTRANSFERASE BISUBSTRATE-INHIBITOR COMPLEX
DBREF  2ZVJ A    1   221  UNP    P22734   COMT_RAT        44    264
SEQADV 2ZVJ GLY A   -1  UNP  P22734              EXPRESSION TAG
SEQADV 2ZVJ SER A    0  UNP  P22734              EXPRESSION TAG
SEQRES   1 A  223  GLY SER MET GLY ASP THR LYS GLU GLN ARG ILE LEU ARG
SEQRES   2 A  223  TYR VAL GLN GLN ASN ALA LYS PRO GLY ASP PRO GLN SER
SEQRES   3 A  223  VAL LEU GLU ALA ILE ASP THR TYR CYS THR GLN LYS GLU
SEQRES   4 A  223  TRP ALA MET ASN VAL GLY ASP ALA LYS GLY GLN ILE MET
SEQRES   5 A  223  ASP ALA VAL ILE ARG GLU TYR SER PRO SER LEU VAL LEU
SEQRES   6 A  223  GLU LEU GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET
SEQRES   7 A  223  ALA ARG LEU LEU GLN PRO GLY ALA ARG LEU LEU THR MET
SEQRES   8 A  223  GLU MET ASN PRO ASP TYR ALA ALA ILE THR GLN GLN MET
SEQRES   9 A  223  LEU ASN PHE ALA GLY LEU GLN ASP LYS VAL THR ILE LEU
SEQRES  10 A  223  ASN GLY ALA SER GLN ASP LEU ILE PRO GLN LEU LYS LYS
SEQRES  11 A  223  LYS TYR ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP
SEQRES  12 A  223  HIS TRP LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU
SEQRES  13 A  223  GLU LYS CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU
SEQRES  14 A  223  ALA ASP ASN VAL ILE VAL PRO GLY THR PRO ASP PHE LEU
SEQRES  15 A  223  ALA TYR VAL ARG GLY SER SER SER PHE GLU CYS THR HIS
SEQRES  16 A  223  TYR SER SER TYR LEU GLU TYR MET LYS VAL VAL ASP GLY
SEQRES  17 A  223  LEU GLU LYS ALA ILE TYR GLN GLY PRO SER SER PRO ASP
SEQRES  18 A  223  LYS SER
HET     MG  A 300       1
HET    SAM  A 301      27
HET    KOM  A 302      19
HETNAM      MG MAGNESIUM ION
HETNAM     SAM S-ADENOSYLMETHIONINE
HETNAM     KOM 7,8-DIHYDROXY-4-PHENYL-2H-CHROMEN-2-ONE
HETSYN     KOM 4-PHENYL-7,8-DIHYDROXYCOUMARINE
FORMUL   2   MG    MG 2+
FORMUL   3  SAM    C15 H22 N6 O5 S
FORMUL   4  KOM    C15 H10 O4
FORMUL   5  HOH   *73(H2 O)
HELIX    1   1 THR A    4  ALA A   17  1                                  14
HELIX    2   2 ASP A   21  LYS A   36  1                                  16
HELIX    3   3 GLY A   43  SER A   58  1                                  16
HELIX    4   4 GLY A   70  ARG A   78  1                                   9
HELIX    5   5 ASN A   92  GLY A  107  1                                  16
HELIX    6   6 ALA A  118  ILE A  123  1                                   6
HELIX    7   7 GLN A  125  ASP A  131  1                                   7
HELIX    8   8 TRP A  143  ASP A  145  5                                   3
HELIX    9   9 ARG A  146  CYS A  157  1                                  12
HELIX   10  10 THR A  176  SER A  186  1                                  11
SHEET    1   A 7 VAL A 112  ASN A 116  0
SHEET    2   A 7 ARG A  85  GLU A  90  1  N  THR A  88   O  THR A 113
SHEET    3   A 7 LEU A  61  LEU A  65  1  N  GLU A  64   O  LEU A  87
SHEET    4   A 7 MET A 137  LEU A 140  1  O  PHE A 139   N  LEU A  63
SHEET    5   A 7 VAL A 165  ALA A 168  1  O  VAL A 165   N  VAL A 138
SHEET    6   A 7 VAL A 204  TYR A 212 -1  O  ALA A 210   N  LEU A 166
SHEET    7   A 7 PHE A 189  TYR A 197 -1  N  GLU A 190   O  ILE A 211
LINK         OD2 ASP A 141                MG    MG A 300     1555   1555  2.02
LINK         OD2 ASP A 169                MG    MG A 300     1555   1555  1.94
LINK         OD1 ASN A 170                MG    MG A 300     1555   1555  1.98
LINK        MG    MG A 300                 O9  KOM A 302     1555   1555  2.36
LINK        MG    MG A 300                 O   HOH A 371     1555   1555  2.05
LINK        MG    MG A 300                 O10 KOM A 302     1555   1555  1.94
CISPEP   1 VAL A  173    PRO A  174          0        -3.94
SITE     1 AC1  5 ASP A 141  ASP A 169  ASN A 170  KOM A 302
SITE     2 AC1  5 HOH A 371
SITE     1 AC2 21 MET A  40  ASN A  41  VAL A  42  GLY A  66
SITE     2 AC2 21 ALA A  67  TYR A  68  TYR A  71  SER A  72
SITE     3 AC2 21 GLU A  90  MET A  91  TYR A  95  GLY A 117
SITE     4 AC2 21 ALA A 118  SER A 119  GLN A 120  ASP A 141
SITE     5 AC2 21 HIS A 142  TRP A 143  ARG A 146  KOM A 302
SITE     6 AC2 21 HOH A 312
SITE     1 AC3 12 MET A  40  ASP A 141  TRP A 143  LYS A 144
SITE     2 AC3 12 ASP A 169  ASN A 170  PRO A 174  GLU A 199
SITE     3 AC3 12  MG A 300  SAM A 301  HOH A 309  HOH A 371
CRYST1   50.448   50.448  167.626  90.00  90.00 120.00 P 32 2 1      6
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      0.019822  0.011444  0.000000        0.00000
SCALE2      0.000000  0.022889  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005966        0.00000
      
PROCHECK
Go to PROCHECK summary
 References