› 3ij1

X-ray diffraction
2.1Å resolution

Crystal structure of Eed in complex with a trimethylated histone H4K20 peptide

Released:
DOI: 10.2210/pdb3ij1/pdb
PDB entry 3ij1 coloured by chain, front view.
PDB entry 3ij1 coloured by chain, side view.
PDB entry 3ij1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Role of the polycomb protein EED in the propagation of repressive histone marks.
Margueron R, Justin N, Ohno K, Sharpe ML, Son J, Drury WJ, Voigt P, Martin SR, Taylor WR, De Marco V, Pirrotta V, Reinberg D, Gamblin SJ
Nature 461 762-7 (2009)
PMID: 19767730

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131011 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Polycomb protein EED Chain: A
Molecule details ›
Chain: A
Length: 365 amino acids
Theoretical weight: 42.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75530 (Residues: 77-441; Coverage: 83%)
Gene name: EED
Sequence domains: WD domain, G-beta repeat
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
Histone H4 Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.44 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P62805 (Residues: 16-26; Coverage: 11%)
Gene names: H4-16, H4/A, H4/B, H4/C, H4/D, H4/E, H4/G, H4/H, H4/I, H4/J, H4/K, H4/M, H4/N, H4/O, H4C1, H4C11, H4C12, H4C13, H4C14, H4C15, H4C16, H4C2, H4C3, H4C4, H4C5, H4C6, H4C8, H4C9, H4F2, H4FA, H4FB, H4FC, H4FD, H4FE, H4FG, H4FH, H4FI, H4FJ, H4FK, H4FM, H4FN, H4FO, HIST1H4A, HIST1H4B, HIST1H4C, HIST1H4D, HIST1H4E, HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4L, HIST2H4, HIST2H4A, HIST2H4B, HIST4H4

Ligands and Environments

No bound ligands
1 modified residue:
Ligand M3L 1 x M3L

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 57.55Å b: 85.321Å c: 91.229Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.204
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

299 review citations

Histone methylation: a dynamic mark in health, disease and inheritance.
Greer et al. (2012)
298 more

1 mention without citation

Role of the polycomb protein EED in the propagation of repressive histone marks.
Margueron et al. (2009)