Structure of PDB 3oe4 Chain A

Receptor sequence
>3oe4A (length=213) Species: 10116 (Rattus norvegicus) [Search protein sequence]
DTKEQRILRYVQQNAKPGDPQSVLEAIDTYCTQKEWAMNVGDAKGQIMDA
VIREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEINPDCAAITQQM
LNFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDTL
LLEKCGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEYMK
VVDGLEKAIYQGP
3D structure
PDB3oe4 Molecular Recognition at the Active Site of Catechol-O-methyltransferase (COMT): Adenine Replacements in Bisubstrate Inhibitors
ChainA
Resolution1.49 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D141 K144 D169 N170 E199
Catalytic site (residue number reindexed from 1) D139 K142 D167 N168 E197
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 D139 D167 N168
BS02 610 A W38 M40 Y68 E90 I91 A118 S119 D141 H142 W143 K144 N170 P174 E199 W36 M38 Y66 E88 I89 A116 S117 D139 H140 W141 K142 N168 P172 E197 MOAD: Ki=34nM
PDBbind-CN: -logKd/Ki=7.47,Ki=34nM
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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3oe4, PDBe:3oe4, PDBj:3oe4
PDBsum3oe4
PubMed21538606
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

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