Structure of PDB 1jr4 Chain A Binding Site BS02

Receptor Information
>1jr4 Chain A (length=212) 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
VVDGLEKAIYQG
Ligand information
Ligand IDCL4
InChIInChI=1S/C19H19N7O8/c20-16-12-17(23-6-22-16)25(7-24-12)19-15(30)14(29)11(34-19)2-1-3-21-18(31)9-4-8(26(32)33)5-10(27)13(9)28/h1-2,4-7,11,14-15,19,27-30H,3H2,(H,21,31)(H2,20,22,23)/b2-1+/t11-,14-,15-,19-/m1/s1
InChIKeyUHHBFOLQOQSPLU-WGRQDFERSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1c(cc(c(c1C(=O)NCC=CC2C(C(C(O2)n3cnc4c3ncnc4N)O)O)O)O)[N+](=O)[O-]
OpenEye OEToolkits 1.5.0c1c(cc(c(c1C(=O)NC\C=C\[C@@H]2[C@H]([C@H]([C@@H](O2)n3cnc4c3ncnc4N)O)O)O)O)[N+](=O)[O-]
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](C=CCNC(=O)c4cc(cc(O)c4O)[N+]([O-])=O)[CH](O)[CH]3O
ACDLabs 10.04[O-][N+](=O)c1cc(c(O)c(O)c1)C(=O)NC/C=C/C4OC(n3cnc2c(ncnc23)N)C(O)C4O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](/C=C/CNC(=O)c4cc(cc(O)c4O)[N+]([O-])=O)[C@@H](O)[C@H]3O
FormulaC19 H19 N7 O8
NameN-{3-[5-(6-AMINO-PURIN-9-YL)-3,4-DIHYDROXY-TETRAHYDRO-FURAN-2-YL]-ALLYL}-2,3-DIHYDROXY-5-NITRO-BENZAMIDE
ChEMBL
DrugBankDB03907
ZINCZINC000034828673
PDB chain1jr4 Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1jr4 X-ray Crystal Structure of a Bisubstrate Inhibitor Bound to the Enzyme Catechol-O-methyltransferase: A Dramatic Effect of Inhibitor Preorganization on Binding Affinity.
Resolution2.63 Å
Binding residue
(original residue number in PDB)		W38 M40 M89 E90 M91 Y95 A118 S119 D141 H142 W143 K144 N170 P174 L198 E199
Binding residue
(residue number reindexed from 1)		W36 M38 M87 E88 M89 Y93 A116 S117 D139 H140 W141 K142 N168 P172 L196 E197
Annotation score1
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:1jr4, PDBe:1jr4, PDBj:1jr4
PDBsum1jr4
PubMed12404486
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

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