Structure analysis

Crystal Structure of the First Bromodomain of Human Brd2 with the inhibitor GW841819X

X-ray diffraction
1.9Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: homo dimer
Accessible surface area: 11300 Å2
Buried surface area: 3800 Å2
Dissociation area: 900 Å2
Dissociation energy (ΔGdiss): 5 kcal/mol
Dissociation entropy (TΔSdiss): 11 kcal/mol
Interface energy (ΔGint): -37 kcal/mol
Symmetry number: 2
Assembly 2
Download    3D Visualisation
Multimeric state: homo dimer
Accessible surface area: 11300 Å2
Buried surface area: 3500 Å2
Dissociation area: 950 Å2
Dissociation energy (ΔGdiss): 3 kcal/mol
Dissociation entropy (TΔSdiss): 12 kcal/mol
Interface energy (ΔGint): -9 kcal/mol
Symmetry number: 2

Macromolecules

Chains: A, B, C
Length: 153 amino acids
Theoretical weight: 17.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P25440 (Residues: 67-200; Coverage: 17%)
Gene names: BRD2, KIAA9001, RING3
Pfam: Bromodomain
InterPro:
CATH: Bromodomain-like

Search similar proteins