PDBe 5azt

X-ray diffraction
3.45Å resolution

Ternary complex of hPPARalpha ligand binding domain, 17-oxoDHA and a SRC1 peptide

Released:
Source organism: Homo sapiens
Primary publication:
17-OxoDHA Is a PPARα/γ Dual Covalent Modifier and Agonist.
ACS Chem. Biol. (2016)
PMID: 27337155

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peroxisome proliferator-activated receptor alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 269 amino acids
Theoretical weight: 30.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07869 (Residues: 201-468; Coverage: 57%)
Gene names: NR1C1, PPAR, PPARA
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor
Nuclear receptor coactivator 1 Chain: C
Molecule details ›
Chain: C
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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P41212
Unit cell:
a: 59.46Å b: 59.46Å c: 317.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.255 0.253 0.308
Expression systems:
  • Escherichia coli
  • Not provided