Structure of PDB 6bp4 Chain A

Receptor sequence
>6bp4A (length=268) Species: 284812 (Schizosaccharomyces pombe 972h-) [Search protein sequence]
SYTHLSFYEKRELFRKKLREIEGPEVTLVNEVDDEPCPSLDFQFISQYRL
TQGVIPPDPNFQSGCNCSGCDLNNPSRCECLDDLDEPTHFAYDAQGRVRA
DTGAVIYECNSFCSCSMECPNRVVQRGRTLPLEIFKTKEKGWGVRSLRFA
PAGTFITCYLGEVITSAEAAKRDKITYLFDLDMFDDASEYTVDAQNYGDV
SRFFNHSCSPNIAIYSAVRNHGFRTIYDLAFFAIKDIQPLEELTFDYAGS
KLRRQCKCGSANCRGWLF
3D structure
PDB6bp4 Automethylation-induced conformational switch in Clr4 (Suv39h) maintains epigenetic stability.
ChainA
Resolution2.7701 Å
3D
structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A C477 C484 C256 C263
BS02 ZN A C260 C262 C268 C276 C65 C67 C70 C78
BS03 ZN A C260 C307 C311 C65 C109 C113
BS04 ZN A C268 C307 C313 C70 C109 C115
BS05 SAM A I379 N409 H410 R475 C477 K478 L488 I175 N205 H206 R254 C256 K257 L267
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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