Function and Biology Details
Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170797 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cbp/p300-interacting transactivator 2
Molecule details ›
Chain: A
Length: 52 amino acids
Theoretical weight: 5.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains: Helix Hairpins
Length: 52 amino acids
Theoretical weight: 5.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q99967 (Residues: 216-259; Coverage: 16%)
Structure domains: Helix Hairpins
Histone acetyltransferase p300
Molecule details ›
Chain: B
Length: 101 amino acids
Theoretical weight: 11.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: TAZ zinc finger
Structure domains: TAZ domain
Length: 101 amino acids
Theoretical weight: 11.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q09472 (Residues: 323-423; Coverage: 4%)
Sequence domains: TAZ zinc finger
Structure domains: TAZ domain
