Structure of PDB 3hvh Chain A Binding Site BS01

Receptor Information
>3hvh 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 ID542
InChIInChI=1S/C26H25FN6O6/c1-28-23-19-24(31-11-30-23)33(12-32-19)26-22(37)21(36)18(39-26)3-2-8-29-25(38)16-9-14(10-17(34)20(16)35)13-4-6-15(27)7-5-13/h2-7,9-12,18,21-22,26,34-37H,8H2,1H3,(H,29,38)(H,28,30,31)/b3-2+/t18-,21-,22-,26-/m1/s1
InChIKeyNSQDVYXOGVOLPV-WKWRZTKWSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CNc1c2c(ncn1)n(cn2)C3C(C(C(O3)C=CCNC(=O)c4cc(cc(c4O)O)c5ccc(cc5)F)O)O
CACTVS 3.341CNc1ncnc2n(cnc12)[CH]3O[CH](C=CCNC(=O)c4cc(cc(O)c4O)c5ccc(F)cc5)[CH](O)[CH]3O
ACDLabs 10.04Fc1ccc(cc1)c2cc(c(O)c(O)c2)C(=O)NC/C=C/C5OC(n4cnc3c(ncnc34)NC)C(O)C5O
OpenEye OEToolkits 1.5.0CNc1c2c(ncn1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)\C=C\CNC(=O)c4cc(cc(c4O)O)c5ccc(cc5)F)O)O
CACTVS 3.341CNc1ncnc2n(cnc12)[C@@H]3O[C@H](/C=C/CNC(=O)c4cc(cc(O)c4O)c5ccc(F)cc5)[C@@H](O)[C@H]3O
FormulaC26 H25 F N6 O6
NameN-[(E)-3-[(2R,3S,4R,5R)-3,4-dihydroxy-5-(6-methylaminopurin-9-yl)oxolan-2-yl]prop-2-enyl]-5-(4-fluorophenyl)-2,3-dihydroxy-benzamide
ChEMBL
DrugBank
ZINCZINC000058639045
PDB chain3hvh Chain A Residue 1 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3hvh Molecular recognition at the active site of catechol-o-methyltransferase: energetically favorable replacement of a water molecule imported by a bisubstrate inhibitor.
Resolution1.3 Å
Binding residue
(original residue number in PDB)		M83 Y111 E133 M134 A161 S162 Q163 D184 H185 W186 K187 R189 N213 P217 L241 E242
Binding residue
(residue number reindexed from 1)		M38 Y66 E88 M89 A116 S117 Q118 D139 H140 W141 K142 R144 N168 P172 L196 E197
Annotation score1
Binding affinityMOAD: Ki=3nM
PDBbind-CN: -logKd/Ki=8.52,Ki=3nM
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:3hvh, PDBe:3hvh, PDBj:3hvh
PDBsum3hvh
PubMed19882607
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

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