› 5wqx

X-ray diffraction
2.29Å resolution

Covalent bond formation of synthetic ligand with hPPARg-LBD

Released:
DOI: 10.2210/pdb5wqx/pdb
PDB entry 5wqx coloured by chain, front view.
PDB entry 5wqx coloured by chain, side view.
PDB entry 5wqx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
On-site reaction for PPARγ modification using a specific bifunctional ligand.
Kojima H, Itoh T, Yamamoto K
Bioorg Med Chem 25 6492-6500 (2017)
PMID: 29097031

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153379 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxisome proliferator-activated receptor gamma Chains: A, B
Molecule details ›
Chains: A, B
Length: 276 amino acids
Theoretical weight: 31.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P37231 (Residues: 232-505; Coverage: 54%)
Gene names: NR1C3, PPARG
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

1 bound ligand:
Ligand T65 1 x T65
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2
Unit cell:
a: 92.91Å b: 61.2Å c: 118.02Å
α: 90° β: 102.82° γ: 90°
R-values:
R R work R free
0.232 0.229 0.277
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Structural basis for the inhibitory effects of a novel reversible covalent ligand on PPARγ phosphorylation.
Jang et al. (2019)