Function and Biology Details
Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156891 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Vacuolar protein sorting-associated protein 75
Molecule details ›
Chains: A, B
Length: 264 amino acids
Theoretical weight: 30.66 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains: Nucleosome assembly protein (NAP)
Length: 264 amino acids
Theoretical weight: 30.66 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical:
P53853 (Residues: 1-264; Coverage: 100%)
Sequence domains: Nucleosome assembly protein (NAP)
Histone acetyltransferase RTT109
Molecule details ›
Chain: C
Length: 442 amino acids
Theoretical weight: 50.81 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains: Histone acetylation protein
Length: 442 amino acids
Theoretical weight: 50.81 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical: Q07794 (Residues: 1-436; Coverage: 100%)
Sequence domains: Histone acetylation protein
