2e3k

X-ray diffraction
2.3Å resolution

Crystal structure of the human Brd2 second bromodomain in complexed with the acetylated histone H4 peptide

Released:
Entry authors: Padmanabhan B, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-135455 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bromodomain-containing protein 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 112 amino acids
Theoretical weight: 13.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P25440 (Residues: 348-455; Coverage: 14%)
Gene names: BRD2, KIAA9001, RING3
Sequence domains: Bromodomain
Structure domains: Bromodomain-like
Histone H4 Chains: Q, R
Molecule details ›
Chains: Q, R
Length: 15 amino acids
Theoretical weight: 1.37 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P02309 (Residues: 2-16; Coverage: 15%)
Gene names: HHF1, HHF2, N2752, YBR009C, YBR0122, YNL030W

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21
Unit cell:
a: 45.828Å b: 128.591Å c: 45.847Å
α: 90° β: 104.7° γ: 90°
R-values:
R R work R free
0.204 0.201 0.268
Expression systems:
  • Escherichia coli
  • Not provided