› 5i86

X-ray diffraction
1.05Å 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
Molecule details ›
Chains: A, B
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 EDO 2 x EDO
Ligand SCN 1 x SCN
Ligand 69A 2 x 69A
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P1
Unit cell:
a: 33.993Å b: 42.002Å c: 49.8Å
α: 96.77° β: 109.7° γ: 99.39°
R-values:
R R work R free
0.14 0.139 0.161
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

3 mentions without citation

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