PDBe 3fli

X-ray diffraction
2Å resolution

Discovery of XL335, a Highly Potent, Selective and Orally-Active Agonist of the Farnesoid X Receptor (FXR)

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bile acid receptor Chain: A
Molecule details ›
Chain: A
Length: 231 amino acids
Theoretical weight: 26.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96RI1 (Residues: 258-486; Coverage: 47%)
Gene names: BAR, FXR, HRR1, NR1H4, RIP14
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P41212
Unit cell:
a: 66.519Å b: 66.519Å c: 125.434Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.19 0.243
Expression system: Escherichia coli