› 5mj5

X-ray diffraction
1.9Å resolution

Crystal structure of the Retinoid X Receptor alpha in complex with synthetichonokiol derivative 3 and a fragment of the TIF2 co-activator.

Released:
DOI: 10.2210/pdb5mj5/pdb
PDB entry 5mj5 coloured by chain, front view.
PDB entry 5mj5 coloured by chain, side view.
PDB entry 5mj5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Ligand Dependent Switch from RXR Homo- to RXR-NURR1 Heterodimerization.
Scheepstra M, Andrei SA, de Vries RMJM, Meijer FA, Ma JN, Burstein ES, Olsson R, Ottmann C, Milroy LG, Brunsveld L
ACS Chem Neurosci 8 2065-2077 (2017)
PMID: 28691794

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148720 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Retinoic acid receptor RXR-alpha Chain: A
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 25.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19793 (Residues: 229-457; Coverage: 50%)
Gene names: NR2B1, RXRA
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor
LYS-HIS-LYS-ILE-LEU-HIS-ARG-LEU-LEU-GLN-ASP-SER Chain: B
Molecule details ›
Chain: B
Length: 13 amino acids
Theoretical weight: 1.58 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand 7O0 1 x 7O0
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, DESY BEAMLINE P11
Spacegroup: P43212
Unit cell:
a: 68.159Å b: 68.159Å c: 109.719Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.197 0.243
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 review citations

Nuclear receptor crosstalk - defining the mechanisms for therapeutic innovation.
De Bosscher et al. (2020)
1 more

2 mentions without citation

Targeting SARS-CoV-2 Proteases for COVID-19 Antiviral Development.
Lv et al. (2021)
1 more