› 7bq1

X-ray diffraction
1.52Å resolution

X-ray structure of human PPARalpha ligand binding domain-intrinsic fatty acid (E. coli origin)-SRC1 coactivator peptide co-crystals obtained by co-crystallization

Released:
DOI: 10.2210/pdb7bq1/pdb
Model geometry
Fit model/data
PDB entry 7bq1 coloured by chain, front view.
PDB entry 7bq1 coloured by chain, side view.
PDB entry 7bq1 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

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170553 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
Nuclear receptor coactivator 1 Chain: B
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.85 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15788 (Residues: 683-697; Coverage: 1%)
Gene names: BHLHE74, NCOA1, SRC1

Ligands and Environments

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

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P21
Unit cell:
a: 44.963Å b: 61.596Å c: 53.229Å
α: 90° β: 106.62° γ: 90°
R-values:
R R work R free
0.195 0.194 0.213
Expression systems:
  • Escherichia coli
  • Not provided

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