› 3jzg

X-ray diffraction
2.1Å resolution

Structure of EED in complex with H3K27me3

Released:
DOI: 10.2210/pdb3jzg/pdb
PDB entry 3jzg coloured by chain, front view.
PDB entry 3jzg coloured by chain, side view.
PDB entry 3jzg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2).
Xu C, Bian C, Yang W, Galka M, Ouyang H, Chen C, Qiu W, Liu H, Jones AE, MacKenzie F, Pan P, Li SS, Wang H, Min J
Proc Natl Acad Sci U S A 107 19266-71 (2010)
PMID: 20974918

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131017 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Polycomb protein EED Chain: A
Molecule details ›
Chain: A
Length: 402 amino acids
Theoretical weight: 46.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75530 (Residues: 40-441; Coverage: 91%)
Gene name: EED
Sequence domains: WD domain, G-beta repeat
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
HISTONE PEPTIDE Chain: B
Molecule details ›
Chain: B
Length: 4 amino acids
Theoretical weight: 505 Da
Source organism: Homo sapiens
Expression system: Not provided

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 FR-E+ DW
Spacegroup: P212121
Unit cell:
a: 57.775Å b: 85.263Å c: 91.169Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.158 0.222
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

50 review citations

Occupying chromatin: Polycomb mechanisms for getting to genomic targets, stopping transcriptional traffic, and staying put.
Simon et al. (2013)
49 more

7 mentions without citation

Readers of histone modifications.
Yun et al. (2011)
6 more