2ygv

X-ray diffraction
2.94Å resolution

Conserved N-terminal domain of the yeast Histone Chaperone Asf1 in complex with the C-terminal fragment of Rad53

Released:

Function and Biology Details

Reaction catalysed:
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
Biochemical function:
  • not assigned
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-540061 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone chaperone ASF1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 158 amino acids
Theoretical weight: 17.87 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P32447 (Residues: 1-156; Coverage: 56%)
Gene names: ASF1, CIA1, J0755, YJL115W
Sequence domains: ASF1 like histone chaperone
Structure domains: Histone chaperone ASF1-like
Serine/threonine-protein kinase RAD53 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 22 amino acids
Theoretical weight: 2.5 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
  • Canonical: P22216 (Residues: 800-821; Coverage: 3%)
Gene names: MEC2, P2588, RAD53, SAD1, SPK1, YPL153C

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: C2
Unit cell:
a: 125.24Å b: 98.18Å c: 86.49Å
α: 90° β: 132.49° γ: 90°
R-values:
R R work R free
0.191 0.188 0.257
Expression systems:
  • Escherichia coli BL21
  • Not provided