Structure analysis

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

X-ray diffraction
2.799Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero trimer (preferred)
Entry contents: 3 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 18072.51 Å2
Buried surface area: 13932.39 Å2
Dissociation area: 3,608.04 Å2
Dissociation energy (ΔGdiss): 65.46 kcal/mol
Dissociation entropy (TΔSdiss): 12.35 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-158676

Macromolecules

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
Pfam: Death domain-associated protein 6, histone binding domain
InterPro:
CATH: Methane Monooxygenase Hydroxylase; Chain G, domain 1

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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, H3.3A, H3.3B, H3F3, H3F3A, H3F3B, PP781
Pfam: Core histone H2A/H2B/H3/H4
InterPro:
CATH: Histone, subunit A

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