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5P9A

rat catechol O-methyltransferase in complex with N-[2-[2-(6-aminopurin-9-yl)ethoxy]ethyl]-5-(4-fluorophenyl)-2,3-dihydroxybenzamide at 1.91A

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
A77N302
AHOH436

site_idAC2
Number of Residues25
Detailsbinding site for residue 77N A 302
ChainResidue
AMET91
AALA97
AGLN100
AGLN101
AGLY117
AALA118
ASER119
AGLN120
AASP141
AHIS142
ATRP143
ALYS144
AASP169
AASN170
AGLU199
AMG301
AD1D303
AHOH436
AHOH453
AHOH487
AHOH501
ATRP38
AMET40
AMET89
AGLU90

site_idAC3
Number of Residues6
Detailsbinding site for residue D1D A 303
ChainResidue
ATRP38
AALA96
AGLN100
AILE114
AMET201
A77N302

site_idAC4
Number of Residues3
Detailsbinding site for residue K A 304
ChainResidue
AASN41
AVAL42
ASER72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12237326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {}
ChainResidueDetails

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

246704

PDB entries from 2025-12-24

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