Peroxisome proliferator-activated receptor alpha (PPARA) is a 468-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q07869.
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The mean pLDDT of this model is 80.2 (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 | 65% |
| 70 to 90 | Confident: backbone generally right | 10% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 22% |
What pLDDT means and how to read it
Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as a transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2
Heterodimer; with RXRA. This heterodimerization is required for DNA binding and transactivation activity. Interacts with NCOA3 coactivator. Interacts with CITED2; the interaction stimulates its transcriptional activity. Also interacts with PPARBP in vitro. Interacts with AKAP13, LPIN1, PRDM16 and coactivator NCOA6. Interacts with ASXL1 and ASXL2. Interacts with PER2. Interacts with SIRT1; the…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6KAX | X-ray | 1.23 Å | A=200-468 |
| 6LXA | X-ray | 1.23 Å | A=200-468 |
| 6KB1 | X-ray | 1.25 Å | A=200-468 |
| 6LX6 | X-ray | 1.3 Å | A=200-468 |
| 6KB0 | X-ray | 1.35 Å | A=200-468 |
| 9IWM | X-ray | 1.39 Å | A=200-468 |
| 6LX9 | X-ray | 1.4 Å | A=200-468 |
| 6LX7 | X-ray | 1.41 Å | A=200-468 |
| 6KB4 | X-ray | 1.42 Å | A=200-468 |
| 6KB6 | X-ray | 1.43 Å | A=200-468 |
| 6KB3 | X-ray | 1.45 Å | A=200-468 |
| 6KB8 | X-ray | 1.47 Å | A=200-468 |
| 6KAZ | X-ray | 1.48 Å | A=200-468 |
| 9IWO | X-ray | 1.49 Å | A=200-468 |
| 7BQ1 | X-ray | 1.52 Å | A=200-468 |
| 7BQ2 | X-ray | 1.52 Å | A=200-468 |
| 6LX8 | X-ray | 1.54 Å | A=200-468 |
| 6KB9 | X-ray | 1.55 Å | A=200-468 |
| 7E5I | X-ray | 1.58 Å | A=200-468 |
| 8YT9 | X-ray | 1.59 Å | A=200-468 |
Showing 20 of 77 experimental structures (best resolution first).
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