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PDBsum entry 3a7e

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Transferase PDB id
3a7e
Jmol
Contents
Protein chain
212 a.a.
Ligands
SAM
DNC
Metals
_MG
Waters ×46
HEADER    TRANSFERASE                             26-SEP-09   3A7E
TITLE     CRYSTAL STRUCTURE OF HUMAN COMT COMPLEXED WITH SAM AND 3,5-
TITLE    2 DINITROCATECHOL
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 51-264;
COMPND   5 EC: 2.1.1.6;
COMPND   6 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: COMT;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 CODON PLUS (DE3) RP;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS    COMT, ALTERNATIVE INITIATION, CATECHOLAMINE METABOLISM, MAGNESIUM,
KEYWDS   2 METHYLTRANSFERASE, NEUROTRANSMITTER DEGRADATION, S-ADENOSYL-L-
KEYWDS   3 METHIONINE, TRANSFERASE, CELL MEMBRANE, MEMBRANE, METAL-BINDING,
KEYWDS   4 PHOSPHOPROTEIN, SIGNAL-ANCHOR, TRANSMEMBRANE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.TSUJI
REVDAT   1   15-SEP-10 3A7E    0
JRNL        AUTH   Y.NONAKA,T.MOMOSE,T.OZAWA,M.OZAWA,M.NAKATSU,E.TSUJI,
JRNL        AUTH 2 K.OKAZAKI,Y.TAKASE,T.KIYOTANI
JRNL        TITL   HIT TO LEAD: COMPREHENSIVE STRATEGY OF DE NOVO SCAFFOLD
JRNL        TITL 2 GENERATION BY FBDD. PART 1: IN SILICO FRAGMENTS LINKING AND
JRNL        TITL 3 VERIFICATION OF SPATIAL PROXIMITY USING INTER LIGAND NOE
JRNL        TITL 4 APPROACHS
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0072
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) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 5888
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) : 0.226
REMARK   3   R VALUE            (WORKING SET) : 0.218
REMARK   3   FREE R VALUE                     : 0.298
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 654
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) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 394
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1990
REMARK   3   BIN FREE R VALUE SET COUNT          : 46
REMARK   3   BIN FREE R VALUE                    : 0.3430
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1660
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 42
REMARK   3   SOLVENT ATOMS            : 46
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 38.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.50
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.19000
REMARK   3    B22 (A**2) : 0.19000
REMARK   3    B33 (A**2) : -0.29000
REMARK   3    B12 (A**2) : 0.10000
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): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.471
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.353
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.410
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.899
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.821
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1733 ; 0.005 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2352 ; 0.912 ; 2.001
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   211 ; 4.475 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    76 ;34.618 ;24.868
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   301 ;18.171 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;16.248 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   267 ; 0.067 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1297 ; 0.003 ; 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):  1059 ; 0.604 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1707 ; 1.195 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   674 ; 1.910 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   645 ; 3.184 ; 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   : 1.40
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 RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3A7E COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB028904.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : 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) : 1.54180
REMARK 200  MONOCHROMATOR                  : SI 111
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   : 6727
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 3.400
REMARK 200  R MERGE                    (I) : 0.16300
REMARK 200  R SYM                      (I) : 0.13700
REMARK 200   FOR THE DATA SET  : 4.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.33400
REMARK 200  R SYM FOR SHELL            (I) : 0.35200
REMARK 200   FOR SHELL         : 12.700
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   (%): 53.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH7.5, 2% (V/V) PEG 400,
REMARK 280  2.0M (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 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      112.12400
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       56.06200
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       56.06200
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      112.12400
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 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   CD1  ILE A    89     O    HOH A   263              2.03
REMARK 500   NE2  HIS A    12     O    HOH A   260              2.09
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      -59.47   -125.45
REMARK 500    MET A  40       39.14    -75.40
REMARK 500    GLN A  58       67.55     38.90
REMARK 500    TYR A  68     -106.52     65.08
REMARK 500    ASP A 131       77.26     51.51
REMARK 500    ASP A 133      -85.91    -93.34
REMARK 500    ASP A 141       23.60   -158.52
REMARK 500    HIS A 142     -152.44    -85.62
REMARK 500    SER A 196     -146.62   -139.32
REMARK 500    ASP A 205     -168.67   -118.13
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 215  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141   OD2
REMARK 620 2 ASP A 169   OD2  85.3
REMARK 620 3 ASN A 170   OD1  87.9  85.7
REMARK 620 4 DNC A 217   O2   90.7 163.8  78.5
REMARK 620 5 DNC A 217   O1  160.9 104.2  76.5  75.5
REMARK 620 6 ASP A 141   OD1  50.1  82.5 137.1 106.8 146.4
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 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DNC A 217
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3A7D   RELATED DB: PDB
REMARK 900 RAT CATECHOL-O-METHYLTRANSFERASE COMPLEXED WITH BI-
REMARK 900 SUBSTRATE TYPE INHIBITOR
REMARK 900 RELATED ID: 3BWM   RELATED DB: PDB
REMARK 900 HUMAN CATECHOL-O-METHYLTRANSFERASE COMPLEXED WITH SAM AND
REMARK 900 3,5-DINITROCATECHOL
REMARK 900 RELATED ID: 3BWY   RELATED DB: PDB
REMARK 900 HUMAN CATECHOL-O-METHYLTRANSFERASE COMPLEXED WITH SAM AND
REMARK 900 3,5-DINITROCATECHOL
REMARK 900 RELATED ID: 1VID   RELATED DB: PDB
REMARK 900 RAT CATECHOL-O-METHYLTRANSFERASE COMPLEXED WITH SAM AND 3,
REMARK 900 5-DINITROCATECHOL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE IS BASED ON ISOFORM SOLUBLE OF P21964(COMT_HUMAN).
DBREF  3A7E A    1   214  UNP    P21964   COMT_HUMAN      51    264
SEQADV 3A7E GLY A   -1  UNP  P21964              EXPRESSION TAG
SEQADV 3A7E SER A    0  UNP  P21964              EXPRESSION TAG
SEQRES   1 A  216  GLY SER MET GLY ASP THR LYS GLU GLN ARG ILE LEU ASN
SEQRES   2 A  216  HIS VAL LEU GLN HIS ALA GLU PRO GLY ASN ALA GLN SER
SEQRES   3 A  216  VAL LEU GLU ALA ILE ASP THR TYR CYS GLU GLN LYS GLU
SEQRES   4 A  216  TRP ALA MET ASN VAL GLY ASP LYS LYS GLY LYS ILE VAL
SEQRES   5 A  216  ASP ALA VAL ILE GLN GLU HIS GLN PRO SER VAL LEU LEU
SEQRES   6 A  216  GLU LEU GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET
SEQRES   7 A  216  ALA ARG LEU LEU SER PRO GLY ALA ARG LEU ILE THR ILE
SEQRES   8 A  216  GLU ILE ASN PRO ASP CYS ALA ALA ILE THR GLN ARG MET
SEQRES   9 A  216  VAL ASP PHE ALA GLY VAL LYS ASP LYS VAL THR LEU VAL
SEQRES  10 A  216  VAL GLY ALA SER GLN ASP ILE ILE PRO GLN LEU LYS LYS
SEQRES  11 A  216  LYS TYR ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP
SEQRES  12 A  216  HIS TRP LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU
SEQRES  13 A  216  GLU GLU CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU
SEQRES  14 A  216  ALA ASP ASN VAL ILE CYS PRO GLY ALA PRO ASP PHE LEU
SEQRES  15 A  216  ALA HIS VAL ARG GLY SER SER CYS PHE GLU CYS THR HIS
SEQRES  16 A  216  TYR GLN SER PHE LEU GLU TYR ARG GLU VAL VAL ASP GLY
SEQRES  17 A  216  LEU GLU LYS ALA ILE TYR LYS GLY
HET     MG  A 215       1
HET    SAM  A 216      27
HET    DNC  A 217      14
HETNAM      MG MAGNESIUM ION
HETNAM     SAM S-ADENOSYLMETHIONINE
HETNAM     DNC 3,5-DINITROCATECHOL
FORMUL   2   MG    MG 2+
FORMUL   3  SAM    C15 H22 N6 O5 S
FORMUL   4  DNC    C6 H4 N2 O6
FORMUL   5  HOH   *46(H2 O)
HELIX    1   1 THR A    4  ALA A   17  1                                  14
HELIX    2   2 ASN A   21  LYS A   36  1                                  16
HELIX    3   3 GLY A   43  GLN 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  TYR A  130  1                                   6
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 ALA A  176  SER A  186  1                                  11
SHEET    1   A 7 VAL A 112  VAL A 116  0
SHEET    2   A 7 ARG A  85  GLU A  90  1  N  LEU A  86   O  THR A 113
SHEET    3   A 7 VAL A  61  LEU A  65  1  N  GLU A  64   O  ILE A  87
SHEET    4   A 7 LEU A 135  LEU A 140  1  O  PHE A 139   N  LEU A  63
SHEET    5   A 7 LEU A 160  ALA A 168  1  O  LEU A 167   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  PHE A 197 -1  N  THR A 192   O  LYS A 209
LINK         OD2 ASP A 141                MG    MG A 215     1555   1555  2.09
LINK         OD2 ASP A 169                MG    MG A 215     1555   1555  1.99
LINK         OD1 ASN A 170                MG    MG A 215     1555   1555  2.08
LINK        MG    MG A 215                 O2  DNC A 217     1555   1555  1.99
LINK        MG    MG A 215                 O1  DNC A 217     1555   1555  2.58
LINK         OD1 ASP A 141                MG    MG A 215     1555   1555  2.82
CISPEP   1 CYS A  173    PRO A  174          0        -6.73
SITE     1 AC1  5 ASP A 141  ASP A 169  ASN A 170  SAM A 216
SITE     2 AC1  5 DNC A 217
SITE     1 AC2 21 MET A  40  VAL A  42  GLU A  64  GLY A  66
SITE     2 AC2 21 ALA A  67  TYR A  68  TYR A  71  SER A  72
SITE     3 AC2 21 ILE A  89  GLU A  90  ILE A  91  GLY A 117
SITE     4 AC2 21 SER A 119  GLN A 120  ASP A 141  HIS A 142
SITE     5 AC2 21 TRP A 143  ARG A 146   MG A 215  DNC A 217
SITE     6 AC2 21 HOH A 251
SITE     1 AC3 11 TRP A  38  ASP A 141  HIS A 142  TRP A 143
SITE     2 AC3 11 LYS A 144  ASP A 169  ASN A 170  PRO A 174
SITE     3 AC3 11 GLU A 199   MG A 215  SAM A 216
CRYST1   50.909   50.909  168.186  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      0.019643  0.011341  0.000000        0.00000
SCALE2      0.000000  0.022682  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005946        0.00000
      
PROCHECK
Go to PROCHECK summary
 References