PDBe 3dwy

X-ray diffraction
1.98Å resolution

Crystal Structure of the Bromodomain of Human CREBBP

Released:

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
Macromolecule:
CREB-binding protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 119 amino acids
Theoretical weight: 14.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92793 (Residues: 1081-1197; Coverage: 5%)
Gene names: CBP, CREBBP
Sequence domains: Bromodomain
Structure domains: Histone Acetyltransferase; Chain A

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: R3
Unit cell:
a: 121.484Å b: 121.484Å c: 40.378Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.162 0.159 0.219
Expression system: Escherichia coli