› 6axq

X-ray diffraction
1.3Å 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: 13.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92793 (Residues: 1085-1196; Coverage: 5%)
Gene names: CBP, CREBBP
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

2 bound ligands:
Ligand DMS 6 x DMS
Ligand C2Y 4 x C2Y
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Unit cell:
a: 68.71Å b: 69.98Å c: 110.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.2 0.216
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Modulating the masters: chemical tools to dissect CBP and p300 function.
Breen et al. (2018)
4 other articles

1 mention without citation

Cosolvent Simulations with Fragment-Bound Proteins Identify Hot Spots to Direct Lead Growth.
Lal Gupta et al. (2022)