Structure of PDB 3hvi Chain A

Receptor sequence
>3hviA (length=213) Species: 10116 (Rattus norvegicus) [Search protein sequence]
DTKEQRILRYVQQNAKPGDPQSVLEAIDTYCTQKEWAMNVGDAKGQIMDA
VIREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEMNPDYAAITQQM
LNFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDTL
LLEKCGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEYMK
VVDGLEKAIYQGP
3D structure
PDB3hvi Molecular recognition at the active site of catechol-o-methyltransferase: energetically favorable replacement of a water molecule imported by a bisubstrate inhibitor.
ChainA
Resolution1.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D184 K187 D212 N213 E242
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 D184 D212 N213 D139 D167 N168
BS02 619 A W81 M83 Y111 E133 M134 S162 Q163 D184 H185 W186 K187 N213 P217 L241 E242 W36 M38 Y66 E88 M89 S117 Q118 D139 H140 W141 K142 N168 P172 L196 E197 MOAD: Ki=5nM
PDBbind-CN: -logKd/Ki=8.30,Ki=5nM
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
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Biological Process
External links
PDB RCSB:3hvi, PDBe:3hvi, PDBj:3hvi
PDBsum3hvi
PubMed19882607
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

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