› 6lx9

X-ray diffraction
1.4Å resolution

X-ray structure of human PPARalpha ligand binding domain-arachidonic acid co-crystals obtained by delipidation and cross-seeding

Released:
DOI: 10.2210/pdb6lx9/pdb
PDB entry 6lx9 coloured by chain, front view.
PDB entry 6lx9 coloured by chain, side view.
PDB entry 6lx9 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
OpenAccess logo 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 Chain: A
Molecule details ›
Chain: A
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

2 bound ligands:
Ligand GOL 1 x GOL
Ligand ACD 1 x ACD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P21
Unit cell:
a: 44.721Å b: 61.494Å c: 52.874Å
α: 90° β: 106.58° γ: 90°
R-values:
R R work R free
0.174 0.173 0.193
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

2 mentions without citation

PPARα Ligand-Binding Domain Structures with Endogenous Fatty Acids and Fibrates.
Kamata et al. (2020)
1 more