Piezo-type mechanosensitive ion channel component 1 (Piezo1) is a 2547-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: E2JF22.
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The mean pLDDT of this model is 72.5 (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 | 13% |
| 70 to 90 | Confident: backbone generally right | 56% |
| 50 to 70 | Low: treat with caution | 12% |
| Below 50 | Very low: often disordered regions | 19% |
What pLDDT means and how to read it
Pore-forming subunit of the mechanosensitive non-specific cation Piezo channel required for rapidly adapting mechanically activated (MA) currents and has a key role in sensing touch and tactile pain (PubMed:20813920, PubMed:22343900, PubMed:38184690, PubMed:26390154, PubMed:29261642, PubMed:35388220, PubMed:37590348). Piezo channels are homotrimeric three-blade propeller-shaped structures that utilize a cap-motion and plug-and-latch mechanism to gate their ion-conducting pathways (PubMed:26390154, PubMed:29261642, PubMed:35388220, PubMed:37590348). Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium (PubMed:20813920,…
Homotrimer; the homotrimer forms a propeller-shaped Piezo channel with a cation-ion conducting pore (PubMed:26390154, PubMed:29261642, PubMed:35388220, PubMed:37590348). Heterotrimeric interaction may occur between PIEZO1 and PIEZO2 (PubMed:38228630). Interacts with PKD2 (PubMed:24157948). Interacts with STOMl3 (PubMed:24662763). Interacts with TMC1, TMC2, PCDG15 and CIB2; the interaction may be…
Endoplasmic reticulum membrane, Endoplasmic reticulum-Golgi intermediate compartment membrane, Cell membrane, Cell projection, lamellipodium membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4RAX | X-ray | 1.45 Å | A=2214-2457 |
| 7WLT | EM | 3.46 Å | A/C/E=1-2547 |
| 8IMZ | EM | 3.66 Å | A/B/C=1-2547 |
| 11YE | EM | 3.7 Å | C/D/E=1-2547 |
| 6B3R | EM | 3.8 Å | A/C/E=1-2547 |
| 6BPZ | EM | 3.8 Å | A/B/C=1137-2547 |
| 5Z10 | EM | 3.97 Å | A/B/C=1-2547 |
| 8IXO | EM | 4.0 Å | A/B/F=1-2547 |
| 8IXN | EM | 4.07 Å | A/C/D=1-2547 |
| 6LQI | EM | 4.5 Å | A/B/C=1-2547 |
| 3JAC | EM | 4.8 Å | A/B/C=1961-2547 |
| 11ZC | EM | 6.0 Å | A/C/E=1-2547 |
| 7WLU | EM | 6.81 Å | A/C/E=1-2547 |
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