X-ray diffraction
1.54Å resolution

Crystal structure of the first bromodomain of human BRD4 in complex with a tetrahydroquinoline analogue

Source organism: Homo sapiens
Entry authors: Tallant C, Slavish PJ, Siejka P, Bharatham N, Shadrick WR, Chai S, Young BM, Boyd VA, Heroven C, Wiggers HJ, Picaud S, Fedorov O, Krojer T, Chen T, Lee RE, Guy RK, Shelat AA, von Delft F, Arrowsmith CH, Edwards AM, Bountra C, Knapp S, Structural Genomics Consortium (SGC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Bromodomain-containing protein 4 Chain: A
Molecule details ›
Chain: A
Length: 127 amino acids
Theoretical weight: 15.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: O60885 (Residues: 44-168; Coverage: 9%)
Gene names: BRD4, HUNK1
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 38.797Å b: 42.09Å c: 92.576Å
α: 90° β: 90° γ: 90°
R R work R free
0.199 0.197 0.23
Expression system: Escherichia coli