Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) is a 724-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P23727.
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The mean pLDDT of this model is 83.4 (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 | 51% |
| 70 to 90 | Confident: backbone generally right | 35% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling. Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (By…
Heterodimer of a regulatory subunit PIK3R1 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts (via SH2 domains) with CCDC88A/GIV (tyrosine-phosphorylated form); the interaction enables recruitment of PIK3R1 to the EGFR receptor, enhancing PI3K activity and cell migration (By similarity). Interacts with PIK3R2; the interaction is dissociated in an insulin-dependent manner (By…
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1QAD | X-ray | 1.8 Å | A=614-724 |
| 6D85 | X-ray | 2.2 Å | A/B=110-302 |
| 6D81 | X-ray | 2.25 Å | A/B=110-302 |
| 8S3R | X-ray | 2.28 Å | B=431-599 |
| 6D86 | X-ray | 2.3 Å | A/B=110-302 |
| 6MRP | X-ray | 2.4 Å | A/B=110-319 |
| 6D82 | X-ray | 2.41 Å | A/B=110-302 |
| 7JIS | X-ray | 2.42 Å | B=431-599 |
| 8BCY | X-ray | 2.43 Å | B=431-599 |
| 9L3R | X-ray | 2.5 Å | B=431-600 |
| 6OCO | X-ray | 2.58 Å | B=431-600 |
| 5DXU | X-ray | 2.64 Å | B=431-599 |
| 6D87 | X-ray | 2.7 Å | A/B=110-302 |
| 6G6W | X-ray | 2.72 Å | B=431-599 |
| 6OCU | X-ray | 2.77 Å | B=431-600 |
| 9GDI | X-ray | 2.81 Å | B=431-600 |
| 9GCF | X-ray | 2.89 Å | B=431-600 |
| 5T8F | X-ray | 2.91 Å | B=431-599 |
| 5DXH | X-ray | 3.0 Å | B/E=431-599 |
| 6R4R | EM | 3.4 Å | A/B/C/D/E/F/G=1-84 |
Showing 20 of 28 experimental structures (best resolution first).
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