Structure of PDB 4nvq Chain B Binding Site BS02

Receptor Information
>4nvq Chain B (length=263) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRN
ITHLQHCTCVDDCSSSNCLCRCWYDKDGRLLQEFNKIEPPLIFECNQACS
CWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELI
SDAEADVREDDSYLFDLDVYCIDARYYGNISRFINHLCDPNIIPVRVFML
HQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKH
SAEAIALEQSRLA
Ligand information
Ligand ID2OD
InChIInChI=1S/C19H27N3O2/c1-23-16-12-14-15(21-18(20)19(14)6-4-7-19)13-17(16)24-11-5-10-22-8-2-3-9-22/h12-13H,2-11H2,1H3,(H2,20,21)
InChIKeyBKCDJTRMYWSXMC-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O(c2cc1N=C(N)C3(c1cc2OC)CCC3)CCCN4CCCC4
CACTVS 3.385COc1cc2c(cc1OCCCN3CCCC3)N=C(N)C24CCC4
OpenEye OEToolkits 1.7.6COc1cc2c(cc1OCCCN3CCCC3)N=C(C24CCC4)N
FormulaC19 H27 N3 O2
Name5'-methoxy-6'-[3-(pyrrolidin-1-yl)propoxy]spiro[cyclobutane-1,3'-indol]-2'-amine
ChEMBLCHEMBL3109630
DrugBank
ZINCZINC000095921314
PDB chain4nvq Chain B Residue 1202 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4nvq Discovery and development of potent and selective inhibitors of histone methyltransferase g9a.
Resolution2.03 Å
Binding residue
(original residue number in PDB)		Y1067 D1074 A1077 D1078 D1083 S1084 L1086 F1087 D1088 F1152 Y1154 R1157 F1158 I1161
Binding residue
(residue number reindexed from 1)		Y145 D152 A155 D156 D161 S162 L164 F165 D166 F225 Y227 R230 F231 I234
Annotation score1
Binding affinityMOAD: ic50=3.3nM
BindingDB: IC50=3.3nM
Enzymatic activity
Catalytic site (original residue number in PDB) Y1067 Y1154
Catalytic site (residue number reindexed from 1) Y145 Y227
Enzyme Commision number 2.1.1.-
2.1.1.367: [histone H3]-lysine(9) N-methyltransferase.
Gene Ontology
Molecular Function
GO:0002039 p53 binding
GO:0008270 zinc ion binding
GO:0016279 protein-lysine N-methyltransferase activity
GO:0042054 histone methyltransferase activity
Cellular Component
GO:0005634 nucleus

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:4nvq, PDBe:4nvq, PDBj:4nvq
PDBsum4nvq
PubMed24900801
UniProtQ96KQ7|EHMT2_HUMAN Histone-lysine N-methyltransferase EHMT2 (Gene Name=EHMT2)

[Back to BioLiP]