Structure of PDB 3nwb Chain A Binding Site BS02

Receptor Information
>3nwb 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 ID659
InChIInChI=1S/C26H24F2N6O5/c1-29-23-20-24(32-11-31-23)34(12-33-20)26-22(37)19(28)18(39-26)3-2-8-30-25(38)16-9-14(10-17(35)21(16)36)13-4-6-15(27)7-5-13/h2-7,9-12,18-19,22,26,35-37H,8H2,1H3,(H,30,38)(H,29,31,32)/b3-2+/t18-,19+,22-,26-/m1/s1
InChIKeyZHVVVGDBOITDFN-UJYAWEMASA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0CNc1c2c(ncn1)n(cn2)C3C(C(C(O3)C=CCNC(=O)c4cc(cc(c4O)O)c5ccc(cc5)F)F)O
CACTVS 3.370CNc1ncnc2n(cnc12)[CH]3O[CH](C=CCNC(=O)c4cc(cc(O)c4O)c5ccc(F)cc5)[CH](F)[CH]3O
OpenEye OEToolkits 1.7.0CNc1c2c(ncn1)n(cn2)[C@H]3[C@@H]([C@H]([C@H](O3)/C=C/CNC(=O)c4cc(cc(c4O)O)c5ccc(cc5)F)F)O
ACDLabs 12.01Fc1ccc(cc1)c2cc(c(O)c(O)c2)C(=O)NC/C=C/C5OC(n4cnc3c(ncnc34)NC)C(O)C5F
CACTVS 3.370CNc1ncnc2n(cnc12)[C@@H]3O[C@H](\C=C\CNC(=O)c4cc(cc(O)c4O)c5ccc(F)cc5)[C@H](F)[C@H]3O
FormulaC26 H24 F2 N6 O5
NameN-[(E)-3-[(2R,3R,4S,5R)-3-fluoro-4-hydroxy-5-[6-(methylamino)purin-9-yl]oxolan-2-yl]prop-2-enyl]-5-(4-fluorophenyl)-2,3-dihydroxy-benzamide
ChEMBL
DrugBank
ZINCZINC000098208534
PDB chain3nwb Chain A Residue 226 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3nwb Catechol-O-methyltransferase in complex with substituted 3'-deoxyribose bisubstrate inhibitors
Resolution1.3 Å
Binding residue
(original residue number in PDB)		W38 M40 E90 M91 Y95 A118 S119 Q120 D141 H142 W143 K144 N170 P174 L198 E199
Binding residue
(residue number reindexed from 1)		W36 M38 E88 M89 Y93 A116 S117 Q118 D139 H140 W141 K142 N168 P172 L196 E197
Annotation score1
Binding affinityMOAD: ic50=11nM
PDBbind-CN: -logKd/Ki=7.96,IC50=11nM
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:3nwb, PDBe:3nwb, PDBj:3nwb
PDBsum3nwb
PubMed22349227
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

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