Structure of PDB 2cl5 Chain B

Receptor sequence
>2cl5B (length=214) Species: 10116 (Rattus norvegicus) [Search protein sequence]
MGDTKEQRILRYVQQNAKPGDPQSVLEAIDTYCTQKEWAMNVGDAKGQIM
DAVIREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEMNPDYAAITQ
QMLNFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPD
TLLLEKCGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEY
MKVVDGLEKAIYQG
3D structure
PDB2cl5 Comparative Study of Ortho- and Meta-Nitrated Inhibitors of Catechol-O-Methyltransferase: Interactions with the Active Site and Regioselectivity of O-Methylation.
ChainB
Resolution1.6 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) D141 K144 D169 N170 E199
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 BU3 B K36 E37 K36 E37
BS02 MG B D141 D169 N170 D141 D169 N170
BS03 SAM B M40 N41 V42 G66 Y68 Y71 S72 E90 M91 Y95 A118 S119 D141 H142 W143 M40 N41 V42 G66 Y68 Y71 S72 E90 M91 Y95 A118 S119 D141 H142 W143
BS04 BIE B W143 K144 N170 E199 W143 K144 N170 E199
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:2cl5, PDBe:2cl5, PDBj:2cl5
PDBsum2cl5
PubMed16618795
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

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