Structure of PDB 5k0c Chain A

Receptor sequence
>5k0cA (length=215) Species: 10116 (Rattus norvegicus) [Search protein sequence]
GDTKEQRILRYVQQNAKPGDPQSVLEAIDTYCTQKEWAMNVGDAKGQIMD
AVIREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEINPDCAAITQQ
MLNFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDT
LLLEECGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEYM
KVVDGLEKAIYQGPS
3D structure
PDB5k0c Design of Potent and Druglike Nonphenolic Inhibitors for Catechol O-Methyltransferase Derived from a Fragment Screening Approach Targeting the S-Adenosyl-l-methionine Pocket.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D141 K144 D169 N170 E199
Catalytic site (residue number reindexed from 1) D140 K143 D168 N169 E198
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 6OZ A G66 Y68 M89 E90 I91 A118 S119 H142 W143 G65 Y67 M88 E89 I90 A117 S118 H141 W142 PDBbind-CN: -logKd/Ki=5.96,IC50=1.1uM
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5k0c, PDBe:5k0c, PDBj:5k0c
PDBsum5k0c
PubMed27685665
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

[Back to BioLiP]