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 pentamer (preferred)
PDBe Complex ID:
PDB-CPX-139294 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
HTLV-1 basic zipper factor
Molecule details ›
Chains: E, J
Length: 58 amino acids
Theoretical weight: 6.3 KDa
Source organism: Human T-cell leukemia virus type I
Expression system: Escherichia coli
UniProt:
Length: 58 amino acids
Theoretical weight: 6.3 KDa
Source organism: Human T-cell leukemia virus type I
Expression system: Escherichia coli
UniProt:
- Canonical:
P0C746 (Residues: 6-59; Coverage: 26%)
Transcriptional activator Myb
Molecule details ›
Chains: A, C, F, H
Length: 32 amino acids
Theoretical weight: 3.81 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains: LMSTEN motif
Length: 32 amino acids
Theoretical weight: 3.81 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical: P06876 (Residues: 284-315; Coverage: 5%)
Sequence domains: LMSTEN motif
Histone lysine acetyltransferase CREBBP
Molecule details ›
Chains: B, D, G, I
Length: 88 amino acids
Theoretical weight: 10.49 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains: KIX domain
Structure domains: Coactivator CBP, KIX domain
Length: 88 amino acids
Theoretical weight: 10.49 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
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRL BEAMLINE BL9-2
Spacegroup:
P21
Expression system: Escherichia coli
