PDBe 2io5

X-ray diffraction
2.7Å resolution

Crystal structure of the CIA- histone H3-H4 complex

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Histone H4 Chain: C
Molecule details ›
Chain: C
Length: 102 amino acids
Theoretical weight: 11.26 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
  • Canonical: P62799 (Residues: 2-103; Coverage: 99%)
Sequence domains: Centromere kinetochore component CENP-T histone fold
Structure domains: Histone, subunit A
Histone H3.2 Chain: B
Molecule details ›
Chain: B
Length: 135 amino acids
Theoretical weight: 15.29 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
  • Canonical: P84233 (Residues: 2-136; Coverage: 99%)
Structure domains: Histone, subunit A
Histone chaperone ASF1A Chain: A
Molecule details ›
Chain: A
Length: 175 amino acids
Theoretical weight: 19.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y294 (Residues: 1-172; Coverage: 84%)
Gene names: ASF1A, CGI-98, HSPC146
Sequence domains: ASF1 like histone chaperone
Structure domains: ASF1-like

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2221
Unit cell:
a: 97.361Å b: 104.78Å c: 86.48Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.238 0.293
Expression system: Escherichia coli