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:
- Nuclear receptor coactivator, interlocking
- Nucleolar pre-ribosomal-associated protein 1, N-terminal
- Nuclear receptor coactivator, CREB-bp-like, interlocking
- Nuclear receptor coactivator, CREB-bp-like, interlocking domain superfamily
- Nuclear receptor coactivator, Ncoa-type, interlocking
- Nuclear receptor coactivator
- Nuclear receptor coactivator, Ncoa-type, interlocking domain superfamily
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
CREB-binding protein (preferred)
PDBe Complex ID:
PDB-CPX-553294 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
CREB-binding protein
Molecule details ›
Chain: B
Length: 50 amino acids
Theoretical weight: 5.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Creb binding
Structure domains: Nuclear receptor coactivator, CREB-bp-like, interlocking domain
Length: 50 amino acids
Theoretical weight: 5.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q92793 (Residues: 2061-2105; Coverage: 2%)
Sequence domains: Creb binding
Structure domains: Nuclear receptor coactivator, CREB-bp-like, interlocking domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
71%
Refinement method:
simulated annealing
Expression system: Escherichia coli
