› 2i32

X-ray diffraction
2.7Å resolution

Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly

Released:
DOI: 10.2210/pdb2i32/pdb
PDB entry 2i32 coloured by chain, front view.
PDB entry 2i32 coloured by chain, side view.
PDB entry 2i32 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly.
Tang Y, Poustovoitov MV, Zhao K, Garfinkel M, Canutescu A, Dunbrack R, Adams PD, Marmorstein R
Nat Struct Mol Biol 13 921-9 (2006)
PMID: 16980972

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156961 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone chaperone ASF1A Chains: A, B
Molecule details ›
Chains: A, B
Length: 182 amino acids
Theoretical weight: 20.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y294 (Residues: 1-157; Coverage: 77%)
Gene names: ASF1A, CGI-98, HSPC146
Sequence domains: ASF1 like histone chaperone
Structure domains: Histone chaperone ASF1-like
Protein HIRA Chains: E, F
Molecule details ›
Chains: E, F
Length: 57 amino acids
Theoretical weight: 6.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P54198 (Residues: 425-472; Coverage: 5%)
Gene names: DGCR1, HIR, HIRA, TUPLE1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P6522
Unit cell:
a: 116.226Å b: 116.226Å c: 167.599Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.229 0.269
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Histone chaperones: an escort network regulating histone traffic.
De Koning et al. (2007)
26 more

8 mentions without citation

Histone chaperone networks shaping chromatin function.
Hammond et al. (2017)
7 more