Structure of PDB 6bp4 Chain A Binding Site BS01

Receptor Information
>6bp4 Chain A (length=268) Species: 284812 (Schizosaccharomyces pombe 972h-) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SYTHLSFYEKRELFRKKLREIEGPEVTLVNEVDDEPCPSLDFQFISQYRL
TQGVIPPDPNFQSGCNCSGCDLNNPSRCECLDDLDEPTHFAYDAQGRVRA
DTGAVIYECNSFCSCSMECPNRVVQRGRTLPLEIFKTKEKGWGVRSLRFA
PAGTFITCYLGEVITSAEAAKRDKITYLFDLDMFDDASEYTVDAQNYGDV
SRFFNHSCSPNIAIYSAVRNHGFRTIYDLAFFAIKDIQPLEELTFDYAGS
KLRRQCKCGSANCRGWLF
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 chain6bp4 Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6bp4 Automethylation-induced conformational switch in Clr4 (Suv39h) maintains epigenetic stability.
Resolution2.7701 Å
Binding residue
(original residue number in PDB)		C477 C484
Binding residue
(residue number reindexed from 1)		C256 C263
Annotation score1
Enzymatic activity
Enzyme Commision number 2.1.1.355: [histone H3]-lysine(9) N-trimethyltransferase.
2.1.1.366: [histone H3]-N(6),N(6)-dimethyl-lysine(9) N-methyltransferase.
2.1.1.367: [histone H3]-lysine(9) N-methyltransferase.
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
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:6bp4, PDBe:6bp4, PDBj:6bp4
PDBsum6bp4
PubMed30051891
UniProtO60016|CLR4_SCHPO Histone-lysine N-methyltransferase, H3 lysine-9 specific (Gene Name=clr4)

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