› 5igm

X-ray diffraction
1.6Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bromodomain-containing protein 9 Chains: A, B
Molecule details ›
Chains: A, B
Length: 123 amino acids
Theoretical weight: 14.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H8M2 (Residues: 134-243; Coverage: 18%)
Gene names: BRD9, UNQ3040/PRO9856
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

1 bound ligand:
Ligand BMF 2 x BMF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21212
Unit cell:
a: 70.177Å b: 125.677Å c: 29.787Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.22 0.266
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Opportunity knocks for uncovering the new function of an understudied nucleosome remodeling complex member, the bromodomain PHD finger transcription factor, BPTF.
Zahid et al. (2021)
5 more

3 mentions without citation

Promiscuous targeting of bromodomains by bromosporine identifies BET proteins as master regulators of primary transcription response in leukemia.
Picaud et al. (2016)
2 more