Structure analysis

Crystal structure of the CIA- histone H3-H4 complex

X-ray diffraction
2.7Å resolution
Source organisms:
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: 15702.98 Å2
Buried surface area: 6854.65 Å2
Dissociation area: 1,337.82 Å2
Dissociation energy (ΔGdiss): 3.74 kcal/mol
Dissociation entropy (TΔSdiss): 11.92 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-158669

Macromolecules

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
Pfam: ASF1 like histone chaperone
InterPro:
CATH: Histone chaperone ASF1-like
SCOP: ASF1-like

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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%)
Pfam: Core histone H2A/H2B/H3/H4
InterPro:
CATH: Histone, subunit A

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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%)
Pfam: Centromere kinetochore component CENP-T histone fold
InterPro:
CATH: Histone, subunit A
SCOP: Nucleosome core histones

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