Structure of PDB 3r6t Chain A Binding Site BS02

Receptor Information
>3r6t 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
VIREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEINPDCAAITQQM
LNFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDTL
LLEKCGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEYMK
VVDGLEKAIYQGP
Ligand information
Ligand IDLU1
InChIInChI=1S/C26H24FN5O5/c1-14-22-24(30-12-29-14)32(13-31-22)26-21(34)11-18(37-26)3-2-8-28-25(36)19-9-16(10-20(33)23(19)35)15-4-6-17(27)7-5-15/h2-7,9-10,12-13,18,21,26,33-35H,8,11H2,1H3,(H,28,36)/b3-2+/t18-,21-,26-/m1/s1
InChIKeyNFOSSDOJFGCEOO-DEAZYUCPSA-N
SMILES
SoftwareSMILES
CACTVS 3.370Cc1ncnc2n(cnc12)[C@@H]3O[C@@H](C[C@H]3O)\C=C\CNC(=O)c4cc(cc(O)c4O)c5ccc(F)cc5
OpenEye OEToolkits 1.7.2Cc1c2c(ncn1)n(cn2)[C@H]3[C@@H](C[C@H](O3)/C=C/CNC(=O)c4cc(cc(c4O)O)c5ccc(cc5)F)O
ACDLabs 12.01Fc1ccc(cc1)c2cc(c(O)c(O)c2)C(=O)NC/C=C/C5OC(n4cnc3c(ncnc34)C)C(O)C5
OpenEye OEToolkits 1.7.2Cc1c2c(ncn1)n(cn2)C3C(CC(O3)C=CCNC(=O)c4cc(cc(c4O)O)c5ccc(cc5)F)O
CACTVS 3.370Cc1ncnc2n(cnc12)[CH]3O[CH](C[CH]3O)C=CCNC(=O)c4cc(cc(O)c4O)c5ccc(F)cc5
FormulaC26 H24 F N5 O5
Name4'-fluoro-4,5-dihydroxy-N-{(2E)-3-[(2S,4R,5R)-4-hydroxy-5-(6-methyl-9H-purin-9-yl)tetrahydrofuran-2-yl]prop-2-en-1-yl}biphenyl-3-carboxamide
ChEMBL
DrugBank
ZINCZINC000098209131
PDB chain3r6t Chain A Residue 307 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3r6t Catechol-O-methyltransferase in complex with substituted 3'-deoxyribose bisubstrate inhibitors.
Resolution1.2 Å
Binding residue
(original residue number in PDB)		W81 M83 E133 I134 S162 D184 H185 W186 K187 N213 P217 L241 E242
Binding residue
(residue number reindexed from 1)		W36 M38 E88 I89 S117 D139 H140 W141 K142 N168 P172 L196 E197
Annotation score1
Binding affinityMOAD: ic50=1368nM
PDBbind-CN: -logKd/Ki=5.86,IC50=1.368uM
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
View graph for
Biological Process
External links
PDB RCSB:3r6t, PDBe:3r6t, PDBj:3r6t
PDBsum3r6t
PubMed22349227
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

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