› 4mi5

X-ray diffraction
2Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(27) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(27)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172436 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase EZH2 Chain: A
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 25.97 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q15910 (Residues: 521-746; Coverage: 30%)
Gene names: EZH2, KMT6
Sequence domains:
Structure domains: SET domain

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand ZN 6 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P212121
Unit cell:
a: 45.134Å b: 57.674Å c: 75.501Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.196 0.257
Expression system: Spodoptera frugiperda

Quick links

Citations

20 review citations

PRC2 is high maintenance.
Yu et al. (2019)
19 more

17 mentions without citation

Lung Cancer Therapy Targeting Histone Methylation: Opportunities and Challenges.
Chen et al. (2018)
16 more