Structure of PDB 4pyl Chain A

Receptor sequence
>4pylA (length=213) Species: 10116 (Rattus norvegicus) [Search protein sequence]
TKEQRILRYVQQNAKPGDPQSVLEAIDTYCTQKEWAMNVGDAKGQIMDAV
IREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEMNPDYAAITQQML
NFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLL
LEKCGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEYMKV
VDGLEKAIYQGPS
3D structure
PDB4pyl Mapping the conformational space accessible to catechol-O-methyltransferase.
ChainA
Resolution2.2 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) 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 D184 D212 N213 D138 D166 N167
BS02 SFG A M83 N84 V85 G109 Y111 Y114 S115 E133 M134 Y138 A161 S162 D184 H185 W186 M37 N38 V39 G63 Y65 Y68 S69 E87 M88 Y92 A115 S116 D138 H139 W140
BS03 TCW A W81 M83 D184 W186 K187 N213 P217 E242 W35 M37 D138 W140 K141 N167 P171 E196 BindingDB: IC50=2.2nM
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:4pyl, PDBe:4pyl, PDBj:4pyl
PDBsum4pyl
PubMed25084335
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

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