3aad

X-ray diffraction
3.3Å resolution

Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone modifications and site-specific histone eviction

Released:

Function and Biology Details

Reactions catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-149354 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transcription initiation factor TFIID subunit 1 Chain: A
Molecule details ›
Chain: A
Length: 292 amino acids
Theoretical weight: 34.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P21675 (Residues: 1363-1650; Coverage: 15%)
Gene names: BA2R, CCG1, CCGS, TAF1, TAF2A
Sequence domains: Bromodomain
Structure domains: Bromodomain-like
Histone chaperone ASF1A Chains: B, D
Molecule details ›
Chains: B, D
Length: 158 amino acids
Theoretical weight: 17.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y294 (Residues: 1-155; Coverage: 76%)
Gene names: ASF1A, CGI-98, HSPC146
Sequence domains: ASF1 like histone chaperone
Structure domains: Histone chaperone ASF1-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P6122
Unit cell:
a: 102.12Å b: 102.12Å c: 271.92Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.24 0.237 0.293
Expression system: Escherichia coli BL21(DE3)