X-ray diffraction
1.89Å resolution

Crystal structure of the second bromodomain of human BRD2 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 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 114 amino acids
Theoretical weight: 13.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P25440 (Residues: 344-455; Coverage: 14%)
Gene names: BRD2, KIAA9001, RING3
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: C2
Unit cell:
a: 147.244Å b: 94.409Å c: 38.585Å
α: 90° β: 95.43° γ: 90°
R R work R free
0.184 0.181 0.233
Expression system: Escherichia coli