Structure of PDB 3mo2 Chain A Binding Site BS05

Receptor Information
>3mo2 Chain A (length=255) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IVSRDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRNITH
LQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHA
CSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGE
LISDSEADVREEDSYLFDLDGEVYCIDARFYGNVSRFINHHCEPNLVPVR
VFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSP
KCRHS
Ligand information
Ligand IDE67
InChIInChI=1S/C31H47N7O2/c1-37(2)17-10-16-33-31-35-27-22-29(40-20-9-5-8-15-32)28(39-3)21-26(27)30(36-31)34-25-13-18-38(19-14-25)23-24-11-6-4-7-12-24/h4,6-7,11-12,21-22,25H,5,8-10,13-20,23,32H2,1-3H3,(H2,33,34,35,36)
InChIKeyKJNBMUDJPFXUTG-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.370COc1cc2c(NC3CCN(CC3)Cc4ccccc4)nc(NCCCN(C)C)nc2cc1OCCCCCN
ACDLabs 12.01O(c4cc1c(nc(nc1NC3CCN(Cc2ccccc2)CC3)NCCCN(C)C)cc4OCCCCCN)C
OpenEye OEToolkits 1.7.0CN(C)CCCNc1nc2cc(c(cc2c(n1)NC3CCN(CC3)Cc4ccccc4)OC)OCCCCCN
FormulaC31 H47 N7 O2
Name7-[(5-aminopentyl)oxy]-N~4~-(1-benzylpiperidin-4-yl)-N~2~-[3-(dimethylamino)propyl]-6-methoxyquinazoline-2,4-diamine
ChEMBL
DrugBank
ZINCZINC000058633450
PDB chain3mo2 Chain A Residue 1 [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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PDB3mo2 Adding a lysine mimic in the design of potent inhibitors of histone lysine methyltransferases.
Resolution2.49 Å
Binding residue
(original residue number in PDB)		D1131 A1134 D1135 R1137 E1138 D1140 S1141 L1143 D1145 Y1211 R1214 F1215
Binding residue
(residue number reindexed from 1)		D154 A157 D158 R160 E161 D163 S164 L166 D168 Y231 R234 F235
Annotation score1
Binding affinityMOAD: Kd=244nM
PDBbind-CN: -logKd/Ki=6.61,Kd=244nM
Enzymatic activity
Catalytic site (original residue number in PDB) Y1124 Y1211
Catalytic site (residue number reindexed from 1) Y147 Y231
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
GO:0046974 histone H3K9 methyltransferase activity
Cellular Component
GO:0005634 nucleus

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:3mo2, PDBe:3mo2, PDBj:3mo2
PDBsum3mo2
PubMed20434463
UniProtQ9H9B1|EHMT1_HUMAN Histone-lysine N-methyltransferase EHMT1 (Gene Name=EHMT1)

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