Small-conductance mechanosensitive channel (mscS) is a 286-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0C0S1.
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The mean pLDDT of this model is 92.6 (very high 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 | 85% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage; as the membrane is depolarized, less tension is required to open the channel and vice versa. The channel is characterized by short bursts of activity that last for a few seconds
Homoheptamer
Cell inner membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9E68 | EM | 2.5 Å | A/B/C/D/E/F/G=1-31 |
| 9H2S | EM | 2.7 Å | A/B/C/D/E/F/G=91-280 |
| 9H2V | EM | 2.8 Å | A/B/C/D/E/F/G=91-280 |
| 6RLD | EM | 2.93 Å | A/B/C/D/E/F/G=1-286 |
| 5AJI | X-ray | 2.99 Å | A/B/C/D/E/F/G=1-286 |
| 9P0N | EM | 2.99 Å | A/B/C/D/E/F/G=1-286 |
| 6PWN | EM | 3.1 Å | A/B/C/D/E/F/G=1-286 |
| 7OO0 | EM | 3.1 Å | A/B/C/D/E/F/G=1-286 |
| 7OO6 | EM | 3.1 Å | A/B/C/D/E/F/G=1-286 |
| 8DDJ | EM | 3.1 Å | A/B/C/D/E/F/G=1-280 |
| 6VYK | EM | 3.2 Å | A/B/C/D/E/F/G=1-286 |
| 6UZH | EM | 3.3 Å | A/B/C/D/E/F/G=1-286 |
| 3UDC | X-ray | 3.36 Å | A/B/C/D/E/F/G=272-286 |
| 6PWO | EM | 3.4 Å | A/B/C/D/E/F/G=1-286 |
| 6VYL | EM | 3.4 Å | A/B/C/D/E/F/G=1-286 |
| 7RAZ | EM | 3.4 Å | A/B/C/D/E/F/G=1-286 |
| 2VV5 | X-ray | 3.45 Å | A/B/C/D/E/F/G=1-286 |
| 2OAU | X-ray | 3.7 Å | A/B/C/D/E/F/G=1-286 |
| 6VYM | EM | 3.7 Å | A/B/C/D/E/F/G=1-286 |
| 7ONL | EM | 3.9 Å | A/B/C/D/E/F/G=1-286 |
Showing 20 of 24 experimental structures (best resolution first).
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