› 4uit

X-ray diffraction
1.3Å resolution

BROMODOMAIN OF HUMAN BRD9 WITH 7-(3,4-dimethoxyphenyl)-2-(4- methanesulfonylpiperazine-1-carbonyl)-5-methyl-4H,5H-thieno-3,2-c- pyridin-4-one

Released:
DOI: 10.2210/pdb4uit/pdb
PDB entry 4uit coloured by chain, front view.
PDB entry 4uit coloured by chain, side view.
PDB entry 4uit coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery of I-BRD9, a Selective Cell Active Chemical Probe for Bromodomain Containing Protein 9 Inhibition.
Theodoulou NH, Bamborough P, Bannister AJ, Becher I, Bit RA, Che KH, Chung CW, Dittmann A, Drewes G, Drewry DH, Gordon L, Grandi P, Leveridge M, Lindon M, Michon AM, Molnar J, Robson SC, Tomkinson NC, Kouzarides T, Prinjha RK, Humphreys PG
J Med Chem 59 1425-39 (2016)
PMID: 25856009

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190676 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bromodomain-containing protein 9 Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 12.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H8M2 (Residues: 134-238; Coverage: 18%)
Gene names: BRD9, UNQ3040/PRO9856
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

1 bound ligand:
Ligand N1D 1 x N1D
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P1
Unit cell:
a: 24.7Å b: 34.11Å c: 39.68Å
α: 70.26° β: 73.8° γ: 74.24°
R-values:
R R work R free
0.153 0.152 0.173
Expression system: Escherichia coli

Quick links

Citations

36 review citations

The SWI/SNF complex in cancer - biology, biomarkers and therapy.
Mittal et al. (2020)
35 more

1 mention without citation

Inhibition of protein interactions: co-crystalized protein-protein interfaces are nearly as good as holo proteins in rigid-body ligand docking.
Belkin et al. (2018)