Structure of PDB 5fhr Chain A

Receptor sequence
>5fhrA (length=213) Species: 10116 (Rattus norvegicus) [Search protein sequence]
DTKEQRILRYVQQNAKPGDPQSVLEAIDTYCTQKEWAMNVGDAKGQIMDA
VIREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEMNPDYAAITQQM
LNFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDTL
LLEKCGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLELMK
VVDGLEKAIYQGP
3D structure
PDB5fhr Effects of Active-Site Modification and Quaternary Structure on the Regioselectivity of Catechol-O-Methyltransferase.
ChainA
Resolution1.63 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 DNC A W81 W186 K187 N213 W36 W141 K142 N168 BindingDB: IC50=12nM
BS02 MG A D184 D212 N213 D139 D167 N168
BS03 SAM A M83 V85 G109 Y111 S115 E133 M134 Y138 A161 S162 D184 H185 W186 M38 V40 G64 Y66 S70 E88 M89 Y93 A116 S117 D139 H140 W141
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:5fhr, PDBe:5fhr, PDBj:5fhr
PDBsum5fhr
PubMed26797714
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

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