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-520082 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone lysine acetyltransferase CREBBP
Molecule details ›
Chain: A
Length: 87 amino acids
Theoretical weight: 10.35 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains: KIX domain
Structure domains: Coactivator CBP, KIX domain
Length: 87 amino acids
Theoretical weight: 10.35 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical:
P45481 (Residues: 586-672; Coverage: 4%)
Sequence domains: KIX domain
Structure domains: Coactivator CBP, KIX domain
Forkhead box protein O3
Molecule details ›
Chain: B
Length: 52 amino acids
Theoretical weight: 5.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 52 amino acids
Theoretical weight: 5.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: O43524 (Residues: 460-483; Coverage: 4%)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
14%
Refinement method:
simulated annealing
Expression system: Escherichia coli
