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5P9T

humanized rat catechol O-methyltransferase in complex with 6-(4-fluorophenyl)-8-hydroxy-3H-quinazolin-4-one

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0006584biological_processcatecholamine metabolic process
A0008171molecular_functionO-methyltransferase activity
A0016206molecular_functioncatechol O-methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 301
ChainResidue
AASP141
AASP169
AASN170
A7JD304
AHOH420

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 302
ChainResidue
AHOH609
AASP44
AALA45
ATYR200
AHOH551

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 303
ChainResidue
APRO82
AGLY83
AARG85
AASP110
ALYS111
ALYS128

site_idAC4
Number of Residues15
Detailsbinding site for residue 7JD A 304
ChainResidue
AMET40
AALA97
AGLN100
AGLN101
AASP141
AHIS142
ATRP143
AASP169
AASN170
AGLU199
AMG301
ASAH305
AD1D306
AHOH420
AHOH489

site_idAC5
Number of Residues20
Detailsbinding site for residue SAH A 305
ChainResidue
AMET40
AASN41
AVAL42
AGLY66
AALA67
ATYR68
ATYR71
ASER72
AGLU90
AILE91
AGLY117
AALA118
ASER119
AGLN120
AASP141
AHIS142
AARG146
A7JD304
AHOH441
AHOH491

site_idAC6
Number of Residues8
Detailsbinding site for residue D1D A 306
ChainResidue
ATRP38
AALA97
AGLN100
AILE114
AMET201
A7JD304
ANHE307
AHOH419

site_idAC7
Number of Residues9
Detailsbinding site for residue NHE A 307
ChainResidue
AGLU37
ATRP38
AGLN100
AILE114
ALEU115
ATYR130
AMET201
AD1D306
AHOH529

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:12237326
ChainResidueDetails
AVAL42
ASER72
AGLU90
AASP141

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019
ChainResidueDetails
AGLU64
AILE91
ASER119

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AGLY117
ALYS144
AASP169
AASN170
AGLU199

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER216
ASER217
ASER221

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 915
ChainResidueDetails
AASP141metal ligand
ALYS144proton shuttle (general acid/base)
AASP169metal ligand
AASN170metal ligand
AGLU199electrostatic stabiliser

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PDB entries from 2024-09-11

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