Structure of PDB 5v9j Chain B Binding Site BS03

Receptor Information
>5v9j Chain B (length=259) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ERIVSRDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRNI
THLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECN
HACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYV
GELISDSEADVREEDSYLFDLDNKGEVYCIDARFYGNVSRFINHHCEPNL
VPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCR
CGSPKCRHS
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 chain5v9j Chain B Residue 1303 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5v9j Crystal structure of catalytic domain of GLP with MS0105
Resolution1.74 Å
Binding residue
(original residue number in PDB)		C1062 C1075 C1105 C1109
Binding residue
(residue number reindexed from 1)		C56 C69 C99 C103
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y1155 Y1242
Catalytic site (residue number reindexed from 1) Y149 Y235
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:5v9j, PDBe:5v9j, PDBj:5v9j
PDBsum5v9j
PubMed
UniProtQ9H9B1|EHMT1_HUMAN Histone-lysine N-methyltransferase EHMT1 (Gene Name=EHMT1)

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