PDBe 2qxv

X-ray diffraction
1.82Å resolution

Structural basis of EZH2 recognition by EED

Released:
Source organism: Mus musculus
Primary publication:
Structural basis of EZH2 recognition by EED.
Structure 15 1306-15 (2007)
PMID: 17937919

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):
Histone-lysine N-methyltransferase EZH2 Chain: B
Molecule details ›
Chain: B
Length: 30 amino acids
Theoretical weight: 3.75 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q61188 (Residues: 39-68; Coverage: 4%)
Gene names: Enx1h, Ezh2
Sequence domains: WD repeat binding protein EZH2
Polycomb protein EED Chain: A
Molecule details ›
Chain: A
Length: 361 amino acids
Theoretical weight: 41.65 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q921E6 (Residues: 81-441; Coverage: 82%)
Gene name: Eed
Sequence domains: WD domain, G-beta repeat
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: P212121
Unit cell:
a: 50.11Å b: 52.74Å c: 127.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 0.218
Expression system: Escherichia coli BL21