Peroxisome proliferator-activated receptor gamma (PPARG) is a 505-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P37231.
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The mean pLDDT of this model is 76.1 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 55% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 28% |
What pLDDT means and how to read it
Ligand-activated transcription factor that forms obligate heterodimers with the retinoic acid receptor and acts as a key regulator of biological processes, such as adipocyte differentiation, lipid metabolism, glucose homeostasis and beta-oxidation of fatty acids (PubMed:16150867, PubMed:20829347, PubMed:23525231, PubMed:8702406, PubMed:8706692, PubMed:9065481). Activated by lipid ligands: binds peroxisome proliferators, such as hypolipidemic drugs, and fatty acids, such as prostaglandin J2 metabolites (PubMed:16150867, PubMed:20829347, PubMed:23525231, PubMed:8702406, PubMed:8706692, PubMed:9065481). Ligand-binding results in a conformational change in the receptor, promoting dissociation…
Heterodimer with retinoic acid receptor, such as RXRA (By similarity). The heterodimer with the retinoic acid receptor RXRA is called adipocyte-specific transcription factor ARF6 (By similarity). Interacts with NCOA6 coactivator, leading to a strong increase in transcription of target genes (PubMed:10681503). Interacts with coactivator PPARBP, leading to a mild increase in transcription of…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9F7W | X-ray | 1.25 Å | A=234-505 |
| 8BF1 | X-ray | 1.36 Å | A=234-505 |
| 9V8G | X-ray | 1.39 Å | A=231-505 |
| 9V8H | X-ray | 1.39 Å | A=231-505 |
| 8FKC | X-ray | 1.42 Å | A=231-505 |
| 6MS7 | X-ray | 1.43 Å | A=234-505 |
| 9V8D | X-ray | 1.44 Å | A=231-505 |
| 3U9Q | X-ray | 1.52 Å | A=236-504 |
| 8B94 | X-ray | 1.55 Å | A/B=231-505 |
| 8DKV | X-ray | 1.59 Å | A=234-505 |
| 3B1M | X-ray | 1.6 Å | A=234-505 |
| 3V9V | X-ray | 1.6 Å | A=234-505 |
| 9F7X | X-ray | 1.63 Å | A=234-505 |
| 3V9T | X-ray | 1.65 Å | A=234-505 |
| 6T1S | X-ray | 1.65 Å | A=231-505 |
| 8B92 | X-ray | 1.66 Å | A/B=231-505 |
| 5Y2T | X-ray | 1.7 Å | A/B=235-505 |
| 9R6I | X-ray | 1.7 Å | A=231-505 |
| 9V8E | X-ray | 1.7 Å | A=231-505 |
| 8B95 | X-ray | 1.72 Å | A/B=231-505 |
Showing 20 of 380 experimental structures (best resolution first).
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