Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5LSA

human catechol O-methyltransferase in complex with SAM and DNC at 1.50A

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
AASP191
AASP219
AASN220
ADNC304
AHOH433

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 302
ChainResidue
AHOH573
AASP94
ALYS95
ATYR250
AHOH456

site_idAC3
Number of Residues21
Detailsbinding site for residue SAM A 303
ChainResidue
AMET90
AASN91
AVAL92
AGLY116
AALA117
ATYR118
ATYR121
ASER122
AILE139
AGLU140
AILE141
AGLY167
AALA168
ASER169
AGLN170
AASP191
AHIS192
ATRP193
ADNC304
AHOH430
AHOH523

site_idAC4
Number of Residues12
Detailsbinding site for residue DNC A 304
ChainResidue
ATRP88
AASP191
AHIS192
ATRP193
ALYS194
AASP219
AASN220
ALEU248
AGLU249
AMG301
ASAM303
AHOH433

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":"18486144","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 Residues6
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18486144","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon