› 5i89

X-ray diffraction
1.07Å 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 Chain: A
Molecule details ›
Chain: A
Length: 118 amino acids
Theoretical weight: 13.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92793 (Residues: 1082-1197; Coverage: 5%)
Gene names: CBP, CREBBP
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

3 bound ligands:
Ligand ACT 1 x ACT
Ligand CA 1 x CA
Ligand 69B 1 x 69B
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: C2
Unit cell:
a: 94.283Å b: 34.321Å c: 40.005Å
α: 90° β: 106.82° γ: 90°
R-values:
R R work R free
0.118 0.116 0.137
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Bromodomain inhibitors and cancer therapy: From structures to applications.
Pérez-Salvia et al. (2017)
9 more

1 mention without citation

Fragment-Based Discovery of a Selective and Cell-Active Benzodiazepinone CBP/EP300 Bromodomain Inhibitor (CPI-637).
Taylor et al. (2016)