Function and Biology Details
Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Histone acetyltransferase p300 and Histone H4 (preferred)
PDBe Complex ID:
PDB-CPX-158670 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Histone acetyltransferase p300
Molecule details ›
Chain: A
Length: 161 amino acids
Theoretical weight: 18.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 161 amino acids
Theoretical weight: 18.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q09472 (Residues: 1047-1168; Coverage: 5%)
Sequence domains:
Histone acetyltransferase p300
Molecule details ›
Chain: B
Length: 168 amino acids
Theoretical weight: 19.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 168 amino acids
Theoretical weight: 19.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q09472 (Residues: 1047-1168; Coverage: 5%)
Sequence domains:
Histone H4
Molecule details ›
Chain: C
Length: 9 amino acids
Theoretical weight: 842 Da
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
Length: 9 amino acids
Theoretical weight: 842 Da
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
- Canonical: P62799 (Residues: 10-17; Coverage: 8%)
