› 4ouf

X-ray diffraction
1.4Å resolution

Crystal Structure of CBP bromodomain

Released:
DOI: 10.2210/pdb4ouf/pdb
PDB entry 4ouf coloured by chain, front view.
PDB entry 4ouf coloured by chain, side view.
PDB entry 4ouf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Binding of the histone chaperone ASF1 to the CBP bromodomain promotes histone acetylation.
Das C, Roy S, Namjoshi S, Malarkey CS, Jones DN, Kutateladze TG, Churchill ME, Tyler JK
Proc Natl Acad Sci U S A 111 E1072-81 (2014)
PMID: 24616510

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: 116 amino acids
Theoretical weight: 13.85 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

2 bound ligands:
Ligand PEG 1 x PEG
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: R3
Unit cell:
a: 121.79Å b: 121.79Å c: 40.71Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.151 0.149 0.191
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Protein lysine acetylation by p300/CBP.
Dancy et al. (2015)
6 more

5 mentions without citation

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