› 3aqa

X-ray diffraction
2.3Å resolution

Crystal structure of the human BRD2 BD1 bromodomain in complex with a BRD2-interactive compound, BIC1

Released:
DOI: 10.2210/pdb3aqa/pdb
PDB entry 3aqa coloured by chain, front view.
PDB entry 3aqa coloured by chain, side view.
PDB entry 3aqa coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Real-time imaging of histone H4K12-specific acetylation determines the modes of action of histone deacetylase and bromodomain inhibitors.
Ito T, Umehara T, Sasaki K, Nakamura Y, Nishino N, Terada T, Shirouzu M, Padmanabhan B, Yokoyama S, Ito A, Yoshida M
Chem Biol 18 495-507 (2011)
PMID: 21513886

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-150461 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bromodomain-containing protein 2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 128 amino acids
Theoretical weight: 15.26 KDa
Source organism: Homo sapiens
Expression system: bacterial cell free system
UniProt:
  • Canonical: P25440 (Residues: 73-194; Coverage: 15%)
Gene names: BRD2, KIAA9001, RING3
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

2 bound ligands:
Ligand BYH 1 x BYH
Ligand MES 1 x MES
1 modified residue:
Ligand MSE 21 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E DW
Spacegroup: C2
Unit cell:
a: 114.597Å b: 55.716Å c: 68.205Å
α: 90° β: 94.17° γ: 90°
R-values:
R R work R free
0.189 0.189 0.245
Expression system: bacterial cell free system

Quick links

Citations

34 review citations

Erasers of histone acetylation: the histone deacetylase enzymes.
Seto et al. (2014)
33 more

2 mentions without citation

Structural features and inhibitors of bromodomains.
Meslamani et al. (2016)
1 more