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-139292 (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
Transcriptional activator Myb
Molecule details ›
Chain: B
Length: 25 amino acids
Theoretical weight: 2.95 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains: LMSTEN motif
Length: 25 amino acids
Theoretical weight: 2.95 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical: P06876 (Residues: 291-315; Coverage: 4%)
Sequence domains: LMSTEN motif
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
initial structures from DYANA and refined in AMBER
Expression system: Escherichia coli
