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:
- Cellular tumor antigen p53, transactivation domain 2
- p53 transactivation domain
- Nucleolar pre-ribosomal-associated protein 1, N-terminal
- Nuclear receptor coactivator, CREB-bp-like, interlocking domain superfamily
- Nuclear receptor coactivator, CREB-bp-like, interlocking
- Nuclear receptor coactivator, interlocking
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138111 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone lysine acetyltransferase CREBBP
Molecule details ›
Chain: A
Length: 59 amino acids
Theoretical weight: 6.57 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains: Creb binding
Structure domains: Nuclear receptor coactivator, CREB-bp-like, interlocking domain
Length: 59 amino acids
Theoretical weight: 6.57 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical:
P45481 (Residues: 2059-2117; Coverage: 2%)
Sequence domains: Creb binding
Structure domains: Nuclear receptor coactivator, CREB-bp-like, interlocking domain
Cellular tumor antigen p53
Molecule details ›
Chain: B
Length: 49 amino acids
Theoretical weight: 5.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Insulin-like, subunit E
Length: 49 amino acids
Theoretical weight: 5.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P04637 (Residues: 13-61; Coverage: 13%)
Sequence domains:
Structure domains: Insulin-like, subunit E
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
simulated annealing, molecular dynamics
Expression system: Escherichia coli
