Structure of PDB 1h1d Chain A

Receptor sequence
>1h1dA (length=213) Species: 10116 (Rattus norvegicus) [Search protein sequence]
DTKEQRILRYVQQNAKPGDPQSVLEAIDTYCTQKEWAMNVGDAKGQIMDA
VIREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEMNPDYAAITQQM
LNFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDTL
LLEKCGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEYMK
VVDGLEKAIYQGP
3D structure
PDB1h1d Kinetics and Crystal Structure of Catechol-O-Methyltransferase Complex with Co-Substrate and a Novel Inhibitor with Potential Therapeutic Application
ChainA
Resolution2.0 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 P215 D139 D167 N168 P213
BS02 SAM A M40 N41 V42 G66 Y68 S72 E90 M91 A118 S119 D141 H142 W143 M38 N39 V40 G64 Y66 S70 E88 M89 A116 S117 D139 H140 W141
BS03 BIA A W38 W143 K144 N170 P174 E199 W36 W141 K142 N168 P172 E197 MOAD: Ki=6nM
PDBbind-CN: -logKd/Ki=8.22,Ki=6.0nM
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:1h1d, PDBe:1h1d, PDBj:1h1d
PDBsum1h1d
PubMed12237326
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

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