› 4a9k

X-ray diffraction
1.81Å resolution

BROMODOMAIN OF HUMAN CREBBP WITH N-(4-hydroxyphenyl)acetamide

Released:
DOI: 10.2210/pdb4a9k/pdb
PDB entry 4a9k coloured by chain, front view.
PDB entry 4a9k coloured by chain, side view.
PDB entry 4a9k coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Fragment-based discovery of bromodomain inhibitors part 1: inhibitor binding modes and implications for lead discovery.
Chung CW, Dean AW, Woolven JM, Bamborough P
J Med Chem 55 576-86 (2012)
PMID: 22136404

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: 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: Bromodomain-like

Ligands and Environments

4 bound ligands:
Ligand EDO 2 x EDO
Ligand TYL 2 x TYL
Ligand SCN 1 x SCN
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: R3
Unit cell:
a: 120.943Å b: 120.943Å c: 40.471Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.162 0.16 0.197
Expression system: Escherichia coli

Quick links

Citations

36 review citations

Targeting bromodomains: epigenetic readers of lysine acetylation.
Filippakopoulos et al. (2014)
35 more

3 mentions without citation

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)
2 more