Function and Biology Details
Reaction catalysed:
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(27) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(27)
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131031 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Polycomb protein EED
Molecule details ›
Chains: A, B
Length: 367 amino acids
Theoretical weight: 42.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: WD domain, G-beta repeat
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
Length: 367 amino acids
Theoretical weight: 42.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
O75530 (Residues: 76-441; Coverage: 83%)
Sequence domains: WD domain, G-beta repeat
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
Histone-lysine N-methyltransferase EZH2
Molecule details ›
Chains: C, D
Length: 29 amino acids
Theoretical weight: 3.62 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Sequence domains: WD repeat binding protein EZH2
Length: 29 amino acids
Theoretical weight: 3.62 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: Q15910 (Residues: 40-68; Coverage: 4%)
Sequence domains: WD repeat binding protein EZH2
