› 2acl

X-ray diffraction
2.8Å resolution

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Retinoic acid receptor RXR-alpha Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 238 amino acids
Theoretical weight: 26.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19793 (Residues: 225-462; Coverage: 52%)
Gene names: NR2B1, RXRA
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor
Oxysterols receptor LXR-alpha Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 244 amino acids
Theoretical weight: 28.19 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Z0Y9 (Residues: 203-445; Coverage: 55%)
Gene names: Lxra, Nr1h3
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

2 bound ligands:
Ligand REA 4 x REA
Ligand L05 4 x L05
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P1
Unit cell:
a: 60.77Å b: 81.95Å c: 111.44Å
α: 88.98° β: 75.2° γ: 78.27°
R-values:
R R work R free
0.22 0.21 0.28
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Ligands of Therapeutic Utility for the Liver X Receptors.
Komati et al. (2017)
1 more

4 mentions without citation

The retinoid X receptors and their ligands.
Dawson et al. (2012)
3 more