› 5i40

X-ray diffraction
1.04Å resolution

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: 102 amino acids
Theoretical weight: 11.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H8M2 (Residues: 138-239; Coverage: 17%)
Gene names: BRD9, UNQ3040/PRO9856
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

3 bound ligands:
Ligand EDO 4 x EDO
Ligand PEG 1 x PEG
Ligand 67N 1 x 67N
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P1
Unit cell:
a: 24.58Å b: 33.745Å c: 39.503Å
α: 70.47° β: 73.32° γ: 74.52°
R-values:
R R work R free
0.133 0.132 0.16
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics.
Ali et al. (2018)
9 more

2 mentions without citation

Iterative Design and Optimization of Initially Inactive Proteolysis Targeting Chimeras (PROTACs) Identify VZ185 as a Potent, Fast, and Selective von Hippel-Lindau (VHL) Based Dual Degrader Probe of BRD9 and BRD7.
Zoppi et al. (2019)
1 more