› 6lx4

X-ray diffraction
2.13Å resolution

X-ray structure of human PPARalpha ligand binding domain-fenofibric acid co-crystals obtained by delipidation and co-crystallization

Released:
DOI: 10.2210/pdb6lx4/pdb
PDB entry 6lx4 coloured by chain, front view.
PDB entry 6lx4 coloured by chain, side view.
PDB entry 6lx4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
PPARα Ligand-Binding Domain Structures with Endogenous Fatty Acids and Fibrates.
Kamata S, Oyama T, Saito K, Honda A, Yamamoto Y, Suda K, Ishikawa R, Itoh T, Watanabe Y, Shibata T, Uchida K, Suematsu M, Ishii I
iScience 23 101727 (2020)
PMID: 33205029

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170552 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxisome proliferator-activated receptor alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 273 amino acids
Theoretical weight: 30.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07869 (Residues: 200-468; Coverage: 58%)
Gene names: NR1C1, PPAR, PPARA
Sequence domains: Ligand-binding domain of nuclear hormone receptor

Ligands and Environments

1 bound ligand:
Ligand F5A 4 x F5A
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 60.941Å b: 100.048Å c: 62.022Å
α: 90° β: 101.61° γ: 90°
R-values:
R R work R free
0.193 0.191 0.23
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Mechanisms Mediating the Regulation of Peroxisomal Fatty Acid Beta-Oxidation by PPARα.
Tahri-Joutey et al. (2021)
3 more

3 mentions without citation

Marine Natural and Nature-Inspired Compounds Targeting Peroxisome Proliferator Activated Receptors (PPARs).
D'Aniello et al. (2023)
2 more