Structure of PDB 1h1d Chain A Binding Site BS03

Receptor Information
>1h1d Chain A (length=213) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DTKEQRILRYVQQNAKPGDPQSVLEAIDTYCTQKEWAMNVGDAKGQIMDA
VIREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEMNPDYAAITQQM
LNFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDTL
LLEKCGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEYMK
VVDGLEKAIYQGP
Ligand information
Ligand IDBIA
InChIInChI=1S/C20H20F3N3O5/c21-20(22,23)14-2-1-3-15(12-14)25-8-6-24(7-9-25)5-4-17(27)13-10-16(26(30)31)19(29)18(28)11-13/h1-3,10-12,28-29H,4-9H2
InChIKeyKVIVJQWOYSWCCZ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Oc1cc(cc(c1O)[N+]([O-])=O)C(=O)CCN2CCN(CC2)c3cccc(c3)C(F)(F)F
OpenEye OEToolkits 1.5.0c1cc(cc(c1)N2CCN(CC2)CCC(=O)c3cc(c(c(c3)O)O)[N+](=O)[O-])C(F)(F)F
ACDLabs 10.04[O-][N+](=O)c3c(O)c(O)cc(C(=O)CCN2CCN(c1cc(ccc1)C(F)(F)F)CC2)c3
FormulaC20 H20 F3 N3 O5
Name1-(3,4,DIHYDROXY-5-NITROPHENYL)-3-{4-[3-(TRIFLUOROMETHYL) PHENYL] PIPERAZIN-1-YL}PROPAN-1-ONE;
BIA 3-335
ChEMBLCHEMBL387347
DrugBankDB03336
ZINCZINC000003975390
PDB chain1h1d Chain A Residue 335 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1h1d Kinetics and Crystal Structure of Catechol-O-Methyltransferase Complex with Co-Substrate and a Novel Inhibitor with Potential Therapeutic Application
Resolution2.0 Å
Binding residue
(original residue number in PDB)		W38 W143 K144 N170 P174 E199
Binding residue
(residue number reindexed from 1)		W36 W141 K142 N168 P172 E197
Annotation score1
Binding affinityMOAD: Ki=6nM
PDBbind-CN: -logKd/Ki=8.22,Ki=6.0nM
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.
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:1h1d, PDBe:1h1d, PDBj:1h1d
PDBsum1h1d
PubMed12237326
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

[Back to BioLiP]