Structure of PDB 1vid Chain A

Receptor sequence
>1vidA (length=213) Species: 10116 (Rattus norvegicus) [Search protein sequence]
TKEQRILRYVQQNAKPGDPQSVLEAIDTYCTQKEWAMNVGDAKGQIMDAV
IREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEMNPDYAAITQQML
NFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLL
LEKCGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEYMKV
VDGLEKAIYQGPS
3D structure
PDB1vid Crystal structure of catechol O-methyltransferase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D141 K144 D169 N170 E199
Catalytic site (residue number reindexed from 1) D138 K141 D166 N167 E196
Enzyme Commision number 2.1.1.6: catechol O-methyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG A D141 D169 N170 D138 D166 N167
BS02 SAM A M40 N41 V42 G66 Y68 Y71 S72 E90 M91 Y95 A118 S119 D141 H142 W143 M37 N38 V39 G63 Y65 Y68 S69 E87 M88 Y92 A115 S116 D138 H139 W140
BS03 DNC A W38 W143 K144 N170 P174 E199 W35 W140 K141 N167 P171 E196 BindingDB: IC50=12nM
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008171 O-methyltransferase activity
GO:0016206 catechol O-methyltransferase activity
Biological Process
GO:0006584 catecholamine metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1vid, PDBe:1vid, PDBj:1vid
PDBsum1vid
PubMed8127373
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

[Back to BioLiP]