Function and Biology Details
Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
- not assigned
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152309 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone chaperone ASF1
Molecule details ›
Chain: A
Length: 172 amino acids
Theoretical weight: 19.33 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: ASF1 like histone chaperone
Structure domains: Histone chaperone ASF1-like
Length: 172 amino acids
Theoretical weight: 19.33 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P32447 (Residues: 2-169; Coverage: 60%)
Sequence domains: ASF1 like histone chaperone
Structure domains: Histone chaperone ASF1-like
Histone acetyltransferase RTT109
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
90%
Refinement method:
simulated annealing
Expression systems:
- Escherichia coli BL21(DE3)
- Not provided
