X-ray diffraction
2.01Å resolution

Crystal structure of CREBBP bromodomain complexed with LB32A

Source organism: Homo sapiens
Entry authors: Bedi RK, Laul E, Nevado C, Caflisch A

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
CREB-binding protein Chain: A
Molecule details ›
Chain: A
Length: 119 amino acids
Theoretical weight: 14.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q92793 (Residues: 1081-1197; Coverage: 5%)
Gene names: CBP, CREBBP
Sequence domains: Bromodomain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: C2
Unit cell:
a: 86.8Å b: 37.38Å c: 41.67Å
α: 90° β: 102.96° γ: 90°
R R work R free
0.181 0.181 0.215
Expression system: Escherichia coli BL21(DE3)