› 5hyk

X-ray diffraction
1.83Å resolution

Crystal structure of the complex PPARalpha/AL26-29

Released:
DOI: 10.2210/pdb5hyk/pdb
PDB entry 5hyk coloured by chain, front view.
PDB entry 5hyk coloured by chain, side view.
PDB entry 5hyk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for PPAR partial or full activation revealed by a novel ligand binding mode.
Capelli D, Cerchia C, Montanari R, Loiodice F, Tortorella P, Laghezza A, Cervoni L, Pochetti G, Lavecchia A
Sci Rep 6 34792 (2016)
PMID: 27708429

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: 272 amino acids
Theoretical weight: 30.72 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
Structure domains: Retinoid X Receptor

Ligands and Environments

1 bound ligand:
Ligand 65W 1 x 65W
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P41212
Unit cell:
a: 63.65Å b: 63.65Å c: 126Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.211 0.262
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Anti-NASH Drug Development Hitches a Lift on PPAR Agonism.
Boeckmans et al. (2019)
4 more

13 mentions without citation

Structural basis for PPAR partial or full activation revealed by a novel ligand binding mode.
Capelli et al. (2016)
12 more