› 5dbm

X-ray diffraction
1.86Å 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
Molecule details ›
Chains: A, B, C
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

1 bound ligand:
Ligand 58N 3 x 58N
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: C2
Unit cell:
a: 110.588Å b: 34.034Å c: 117.727Å
α: 90° β: 103.93° γ: 90°
R-values:
R R work R free
0.175 0.172 0.22
Expression system: Escherichia coli

Quick links

Citations

14 review citations

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

1 mention without citation

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