PDBe 2hue

X-ray diffraction
1.7Å resolution

Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4

Released:

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero hexamer
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Histone H3.2 Chain: B
Molecule details ›
Chain: B
Length: 77 amino acids
Theoretical weight: 8.89 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
  • Canonical: P84233 (Residues: 62-136; Coverage: 55%)
Structure domains: Histone, subunit A
Histone H4 Chain: C
Molecule details ›
Chain: C
Length: 84 amino acids
Theoretical weight: 9.54 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
  • Canonical: P62799 (Residues: 21-103; Coverage: 81%)
Structure domains: Histone, subunit A
Histone chaperone ASF1 Chain: A
Molecule details ›
Chain: A
Length: 175 amino acids
Theoretical weight: 19.66 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P32447 (Residues: 2-169; Coverage: 60%)
Gene names: ASF1, CIA1, J0755, YJL115W
Structure domains: ASF1-like

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P3121
Unit cell:
a: 95.749Å b: 95.749Å c: 110.676Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.209 0.209 0.239
Expression system: Escherichia coli