Structure of PDB 3hvi Chain A Binding Site BS02

Receptor Information
>3hvi 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 ID619
InChIInChI=1S/C27H27FN6O6/c1-2-29-24-20-25(32-12-31-24)34(13-33-20)27-23(38)22(37)19(40-27)4-3-9-30-26(39)17-10-15(11-18(35)21(17)36)14-5-7-16(28)8-6-14/h3-8,10-13,19,22-23,27,35-38H,2,9H2,1H3,(H,30,39)(H,29,31,32)/b4-3+/t19-,22-,23-,27-/m1/s1
InChIKeyNOCNCHHJBSJZFZ-CJLJSIFTSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CCNc1ncnc2n(cnc12)[C@@H]3O[C@H](/C=C/CNC(=O)c4cc(cc(O)c4O)c5ccc(F)cc5)[C@@H](O)[C@H]3O
ACDLabs 10.04Fc1ccc(cc1)c2cc(c(O)c(O)c2)C(=O)NC/C=C/C5OC(n4cnc3c(ncnc34)NCC)C(O)C5O
OpenEye OEToolkits 1.5.0CCNc1c2c(ncn1)n(cn2)C3C(C(C(O3)C=CCNC(=O)c4cc(cc(c4O)O)c5ccc(cc5)F)O)O
OpenEye OEToolkits 1.5.0CCNc1c2c(ncn1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)\C=C\CNC(=O)c4cc(cc(c4O)O)c5ccc(cc5)F)O)O
CACTVS 3.341CCNc1ncnc2n(cnc12)[CH]3O[CH](C=CCNC(=O)c4cc(cc(O)c4O)c5ccc(F)cc5)[CH](O)[CH]3O
FormulaC27 H27 F N6 O6
NameN-[(E)-3-[(2R,3S,4R,5R)-5-(6-ethylaminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]prop-2-enyl]-5-(4-fluorophenyl)-2,3-dihydroxy-benzamide
ChEMBL
DrugBank
ZINCZINC000058650681
PDB chain3hvi Chain A Residue 267 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3hvi Molecular recognition at the active site of catechol-o-methyltransferase: energetically favorable replacement of a water molecule imported by a bisubstrate inhibitor.
Resolution1.2 Å
Binding residue
(original residue number in PDB)		W81 M83 Y111 E133 M134 S162 Q163 D184 H185 W186 K187 N213 P217 L241 E242
Binding residue
(residue number reindexed from 1)		W36 M38 Y66 E88 M89 S117 Q118 D139 H140 W141 K142 N168 P172 L196 E197
Annotation score1
Binding affinityMOAD: Ki=5nM
PDBbind-CN: -logKd/Ki=8.30,Ki=5nM
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.
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
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Biological Process
External links
PDB RCSB:3hvi, PDBe:3hvi, PDBj:3hvi
PDBsum3hvi
PubMed19882607
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

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