› 1tey

Solution NMR

NMR structure of human histone chaperone, ASF1A

Released:
DOI: 10.2210/pdb1tey/pdb
PDB entry 1tey coloured by chain, ensemble of 20 models, front view.
PDB entry 1tey coloured by chain, ensemble of 20 models, side view.
PDB entry 1tey coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the interaction of Asf1 with histone H3 and its functional implications.
Mousson F, Lautrette A, Thuret JY, Agez M, Courbeyrette R, Amigues B, Becker E, Neumann JM, Guerois R, Mann C, Ochsenbein F
Proc Natl Acad Sci U S A 102 5975-80 (2005)
PMID: 15840725

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195117 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone chaperone ASF1A Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 17.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y294 (Residues: 1-156; Coverage: 77%)
Gene names: ASF1A, CGI-98, HSPC146
Sequence domains: ASF1 like histone chaperone
Structure domains: Histone chaperone ASF1-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, torsion angle dynamics followed by cartesian dynamics
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Chromatin challenges during DNA replication and repair.
Groth et al. (2007)
17 more

7 mentions without citation

Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.
Warren et al. (2017)
6 more