› 4bcr

X-ray diffraction
2.5Å resolution

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
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: 274 amino acids
Theoretical weight: 31.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q07869 (Residues: 195-468; Coverage: 59%)
Gene names: NR1C1, PPAR, PPARA
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

2 bound ligands:
Ligand EDO 2 x EDO
Ligand WY1 4 x WY1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P212121
Unit cell:
a: 62.061Å b: 62.359Å c: 180.048Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.216
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

PPAR-α agonists are still on the rise: an update on clinical and experimental findings.
Ferri et al. (2017)
3 more

14 mentions without citation

Development of Heterocyclic PPAR Ligands for Potential Therapeutic Applications.
Virendra et al. (2022)
13 more