PDBe 5u62

X-ray diffraction
1.9Å resolution

Crystal structure of EED in complex with H3K27Me3 peptide and 6-(benzo[d][1,3]dioxol-4-ylmethyl)-5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-3-amine


Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Polycomb protein EED Chains: A, B
Molecule details ›
Chains: A, B
Length: 367 amino acids
Theoretical weight: 42.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
  • Canonical: O75530 (Residues: 76-441; Coverage: 83%)
Gene name: EED
Sequence domains: WD domain, G-beta repeat
Histone-lysine N-methyltransferase EZH2 Chains: C, D
Molecule details ›
Chains: C, D
Length: 30 amino acids
Theoretical weight: 3.75 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: Q15910 (Residues: 39-68; Coverage: 4%)
Gene names: EZH2, KMT6
Sequence domains: WD repeat binding protein EZH2

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 92.881Å b: 178.113Å c: 50.48Å
α: 90° β: 90° γ: 90°
R R work R free
0.17 0.168 0.208
Expression systems:
  • Escherichia coli K-12
  • Not provided