PDBe 5ij7

X-ray diffraction
2.62Å resolution

Structure of Hs/AcPRC2 in complex with a pyridone inhibitor

Released:

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 trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Enhancer of Zeste Homolog 2 (EZH2),Histone-lysine N-methyltransferase EZH2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 643 amino acids
Theoretical weight: 72.94 KDa
Source organism: Anolis carolinensis
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: G1KPH4 (Residues: 4-478, 502-737; Coverage: 85%)
Gene name: EZH2
Sequence domains:
Polycomb protein EED Chains: E, F
Molecule details ›
Chains: E, F
Length: 362 amino acids
Theoretical weight: 41.78 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O75530 (Residues: 80-441; Coverage: 82%)
Gene name: EED
Sequence domains: WD domain, G-beta repeat
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
Polycomb protein SUZ12 Chains: S, T
Molecule details ›
Chains: S, T
Length: 191 amino acids
Theoretical weight: 22.27 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q15022 (Residues: 545-725; Coverage: 25%)
Gene names: CHET9, JJAZ1, KIAA0160, SUZ12
Sequence domains: VEFS-Box of polycomb protein

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 69.575Å b: 115.042Å c: 153.033Å
α: 90° β: 102.53° γ: 90°
R-values:
R R work R free
0.194 0.191 0.238
Expression system: Spodoptera frugiperda