› 4yk0

X-ray diffraction
1.65Å resolution

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187751 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CREB-binding protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 114 amino acids
Theoretical weight: 13.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92793 (Residues: 1083-1196; Coverage: 5%)
Gene names: CBP, CREBBP
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

2 bound ligands:
Ligand 986 4 x 986
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: R3
Unit cell:
a: 122.7Å b: 122.7Å c: 81.17Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.246 0.244 0.269
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Targeting the epigenetic regulation of antitumour immunity.
Hogg et al. (2020)
13 more

3 mentions without citation

Regulatory T Cell Modulation by CBP/EP300 Bromodomain Inhibition.
Ghosh et al. (2016)
2 more