X-ray diffraction
2.3Å resolution

Crystal structure analysis of the N-terminal bromodomain of human BRD2 complexed with acetylated histone H4 peptide


Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
homo dimer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bromodomain-containing protein 2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 122 amino acids
Theoretical weight: 14.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P25440 (Residues: 73-194; Coverage: 15%)
Gene names: BRD2, KIAA9001, RING3
Sequence domains: Bromodomain
Structure domains: Bromodomain-like
Histone H4 Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 15 amino acids
Theoretical weight: 1.37 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
  • Canonical: P02309 (Residues: 2-16; Coverage: 15%)
Gene names: HHF1, HHF2, N2752, YBR009C, YBR0122, YNL030W

Ligands and Environments

No bound ligands
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: C2
Unit cell:
a: 113.533Å b: 55.238Å c: 67.735Å
α: 90° β: 93.92° γ: 90°
R R work R free
0.182 0.18 0.243
Expression systems:
  • Escherichia coli
  • Not provided