PDBe 5wuk

X-ray diffraction
2.03Å resolution

Crystal structure of EED [G255D] in complex with EZH2 peptide and EED226 compound

Released:
Source organism: Homo sapiens
Primary publication:
Split luciferase-based biosensors for characterizing EED binders.
Anal. Biochem. 522 37-45 (2017)
PMID: 28111304

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 Chain: A
Molecule details ›
Chain: A
Length: 366 amino acids
Theoretical weight: 42.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75530 (Residues: 76-441; Coverage: 83%)
Gene name: EED
Sequence domains: WD domain, G-beta repeat
Histone-lysine N-methyltransferase EZH2 Chain: B
Molecule details ›
Chain: B
Length: 28 amino acids
Theoretical weight: 3.54 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15910 (Residues: 41-68; Coverage: 4%)
Gene names: EZH2, KMT6

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 53.1Å b: 80.28Å c: 108.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.16 0.191
Expression systems:
  • Escherichia coli
  • Not provided