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5FHQ

Crystal structure of (WT) Rat Catechol-O-Methyltransferase in complex with AdoMet and 3,5-dinitrocatechol (DNC)

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 Residues21
Detailsbinding site for residue SAM A 301
ChainResidue
AMET40
ATYR95
AGLY117
AALA118
ASER119
AGLN120
AASP141
AHIS142
ATRP143
ADNC302
AHOH453
AVAL42
AHOH489
AHOH532
AGLY66
AALA67
ATYR68
ATYR71
ASER72
AGLU90
AMET91

site_idAC2
Number of Residues11
Detailsbinding site for residue DNC A 302
ChainResidue
ATRP38
AASP141
AHIS142
ATRP143
ALYS144
AASP169
AASN170
ASAM301
AMG303
AHOH416
AHOH431

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 303
ChainResidue
AASP141
AASP169
AASN170
ADNC302
AHOH416

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
AMET91
ASER119

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

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 2024-10-30

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