Structure of PDB 2o8j Chain A Binding Site BS04

Receptor Information
>2o8j Chain A (length=254) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNIT
HLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQ
ACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVG
ELISDAEADVREDDSYLFDLDEVYCIDARYYGNISRFINHLCDPNIIPVR
VFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDYFTCQCGSEKCKH
SAEA
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain2o8j Chain A Residue 1504 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2o8j Structural biology of human H3K9 methyltransferases
Resolution1.8 Å
Binding residue
(original residue number in PDB)		C1115 C1168 C1170 C1175
Binding residue
(residue number reindexed from 1)		C192 C241 C243 C248
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y1067 Y1154
Catalytic site (residue number reindexed from 1) Y148 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
Cellular Component
GO:0005634 nucleus

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Molecular Function
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Cellular Component
External links
PDB RCSB:2o8j, PDBe:2o8j, PDBj:2o8j
PDBsum2o8j
PubMed20084102
UniProtQ96KQ7|EHMT2_HUMAN Histone-lysine N-methyltransferase EHMT2 (Gene Name=EHMT2)

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