PDBe 4hga

X-ray diffraction
2.8Å resolution

Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX

Released:
Source organism: Homo sapiens
Primary publication:
Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX.
Nat. Struct. Mol. Biol. 19 1287-92 (2012)
PMID: 23142979

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Death domain-associated protein 6 Chain: A
Molecule details ›
Chain: A
Length: 213 amino acids
Theoretical weight: 24.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UER7 (Residues: 184-390; Coverage: 28%)
Gene names: BING2, DAP6, DAXX
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1
Histone H3.3 Chain: B
Molecule details ›
Chain: B
Length: 136 amino acids
Theoretical weight: 15.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P84243 (Residues: 1-136; Coverage: 100%)
Gene names: H3.3A, H3.3B, H3F3, H3F3A, H3F3B, PP781
Sequence domains: Core histone H2A/H2B/H3/H4
Structure domains: Histone, subunit A
Histone H4 Chain: C
Molecule details ›
Chain: C
Length: 103 amino acids
Theoretical weight: 11.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62805 (Residues: 1-103; Coverage: 100%)
Gene names: H4/A, H4/B, H4/C, H4/D, H4/E, H4/G, H4/H, H4/I, H4/J, H4/K, H4/M, H4/N, H4/O, H4F2, H4FA, H4FB, H4FC, H4FD, H4FE, H4FG, H4FH, H4FI, H4FJ, H4FK, H4FM, H4FN, H4FO, HIST1H4A, HIST1H4B, HIST1H4C, HIST1H4D, HIST1H4E, HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4L, HIST2H4, HIST2H4A, HIST2H4B, HIST4H4
Sequence domains: Centromere kinetochore component CENP-T histone fold
Structure domains: Histone, subunit A

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P6122
Unit cell:
a: 72.103Å b: 72.103Å c: 323.55Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.208 0.271
Expression system: Escherichia coli