› 6tq1

X-ray diffraction
1.9Å 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)
Assembly name:
PDBe Complex ID:
PDB-CPX-150468 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bromodomain-containing protein 2 Chains: AAA, BBB, CCC
Molecule details ›
Chains: AAA, BBB, CCC
Length: 155 amino acids
Theoretical weight: 18.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P25440 (Residues: 67-200; Coverage: 17%)
  • Best match: P25440-4 (Residues: 1-80)
Gene names: BRD2, KIAA9001, RING3
Sequence domains: Bromodomain

Ligands and Environments

3 bound ligands:
Ligand SO4 3 x SO4
Ligand NUH 3 x NUH
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 114.931Å b: 55.606Å c: 68.023Å
α: 90° β: 94.434° γ: 90°
R-values:
R R work R free
0.172 0.17 0.214
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Recent developments in epigenetic cancer therapeutics: clinical advancement and emerging trends.
Nepali et al. (2021)
6 more

1 mention without citation

Pathogen-driven gene expression patterns lead to a novel approach to the identification of common therapeutic targets.
Hossain et al. (2022)