› 5lj2

X-ray diffraction
1.19Å resolution

N-TERMINAL BROMODOMAIN OF HUMAN BRD4 WITH 5-(5-aminopyridin-3-yl)-8-(((3R,4R)-3-((1,1-dioxidotetrahydro-2H-thiopyran-4-yl)methoxy)piperidin-4-yl)amino)-3-methyl-1,7-naphthyridin-2(1H)-one

Released:
DOI: 10.2210/pdb5lj2/pdb
PDB 5lj2 coloured by chain and viewed from the front.
PDB 5lj2 coloured by chain and viewed from the side.
PDB 5lj2 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
A Chemical Probe for the ATAD2 Bromodomain.
Bamborough P, Chung CW, Demont EH, Furze RC, Bannister AJ, Che KH, Diallo H, Douault C, Grandi P, Kouzarides T, Michon AM, Mitchell DJ, Prinjha RK, Rau C, Robson S, Sheppard RJ, Upton R, Watson RJ
Angew. Chem. Int. Ed. Engl. (2016)
PMID: 27530368

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bromodomain-containing protein 4 Chain: A
Molecule details ›
Chain: A
Length: 127 amino acids
Theoretical weight: 15.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60885 (Residues: 42-168; Coverage: 9%)
Gene names: BRD4, HUNK1
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

2 bound ligands:
Ligand EDO 3 x EDO
Ligand 6XW 1 x 6XW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 37.52Å b: 44.28Å c: 78.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.187 0.208
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Tumor-Promoting ATAD2 and Its Preclinical Challenges.
Liu et al. (2022)
7 more

1 mention without citation

A Chemical Probe for the ATAD2 Bromodomain.
Bamborough et al. (2016)