Structure of PDB 3nw9 Chain A Binding Site BS02

Receptor Information
>3nw9 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 ID637
InChIInChI=1S/C26H24FN5O6/c1-13-20-24(30-11-29-13)32(12-31-20)26-23(36)22(35)19(38-26)3-2-8-28-25(37)17-9-15(10-18(33)21(17)34)14-4-6-16(27)7-5-14/h2-7,9-12,19,22-23,26,33-36H,8H2,1H3,(H,28,37)/b3-2+/t19-,22-,23-,26-/m1/s1
InChIKeyHPSAAEAALHAMSZ-ORAYEHMWSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01Fc1ccc(cc1)c2cc(c(O)c(O)c2)C(=O)NC/C=C/C5OC(n4cnc3c(ncnc34)C)C(O)C5O
OpenEye OEToolkits 1.7.0Cc1c2c(ncn1)n(cn2)C3C(C(C(O3)C=CCNC(=O)c4cc(cc(c4O)O)c5ccc(cc5)F)O)O
OpenEye OEToolkits 1.7.0Cc1c2c(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 3.370Cc1ncnc2n(cnc12)[C@@H]3O[C@H](\C=C\CNC(=O)c4cc(cc(O)c4O)c5ccc(F)cc5)[C@@H](O)[C@H]3O
CACTVS 3.370Cc1ncnc2n(cnc12)[CH]3O[CH](C=CCNC(=O)c4cc(cc(O)c4O)c5ccc(F)cc5)[CH](O)[CH]3O
FormulaC26 H24 F N5 O6
NameN-[(E)-3-[(2R,3S,4R,5R)-3,4-dihydroxy-5-(6-methylpurin-9-yl)oxolan-2-yl]prop-2-enyl]-5-(4-fluorophenyl)-2,3-dihydroxy-benzamide
ChEMBL
DrugBank
ZINCZINC000064746514
PDB chain3nw9 Chain A Residue 228 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3nw9 Molecular Recognition at the Active Site of Catechol-O-methyltransferase (COMT): Adenine Replacements in Bisubstrate Inhibitors
Resolution1.65 Å
Binding residue
(original residue number in PDB)		W38 M40 Y68 E90 M91 A118 S119 D141 H142 W143 K144 N170 P174 L198 E199
Binding residue
(residue number reindexed from 1)		W36 M38 Y66 E88 M89 A116 S117 D139 H140 W141 K142 N168 P172 L196 E197
Annotation score1
Binding affinityMOAD: Ki=1nM
PDBbind-CN: -logKd/Ki=9.00,Ki=1nM
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:3nw9, PDBe:3nw9, PDBj:3nw9
PDBsum3nw9
PubMed21538606
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

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