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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138116 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone acetyltransferase p300
Molecule details ›
Chain: A
Length: 90 amino acids
Theoretical weight: 9.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: TAZ zinc finger
Structure domains: TAZ domain
Length: 90 amino acids
Theoretical weight: 9.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q09472 (Residues: 1723-1812; Coverage: 4%)
Sequence domains: TAZ zinc finger
Structure domains: TAZ domain
Cellular tumor antigen p53
Molecule details ›
Chain: B
Length: 25 amino acids
Theoretical weight: 2.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Transactivation domain 2
Length: 25 amino acids
Theoretical weight: 2.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P04637 (Residues: 35-59; Coverage: 6%)
Sequence domains: Transactivation domain 2
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
82%
Refinement method:
molecular dynamics
Expression system: Escherichia coli
