Cryo-EM structure of mechanosensitive channel MscS in PC-10 nanodiscs. Determined by electron microscopy at 3.4 Å resolution. Released 10 Feb 2021.
Explore 6VYL in 3D Show helices and sheets RCSB PDB PDBe
6VYL contains 56 α-helices and 105 β-strands across 7 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-59 | 32 | |
| α-helix | 65-86 | 22 | |
| α-helix | 93-110 | 18 | |
| α-helix | 116-126 | 11 | |
| β-strand | 135-137 | 3 | 1 |
| β-strand | 142-148 | 7 | 1 |
| β-strand | 152-157 | 6 | 1 |
| β-strand | 162-166 | 5 | 1 |
| α-helix | 167-170 | 4 | |
| β-strand | 175-177 | 3 | 2 |
| β-strand | 183-185 | 3 | 3 |
| β-strand | 188-192 | 5 | 4 |
| α-helix | 198-211 | 14 | |
| β-strand | 215 | 1 | 3 |
| β-strand | 222-228 | 7 | 4 |
| β-strand | 233-238 | 6 | 4 |
| β-strand | 240-242 | 3 | 3 |
| α-helix | 246-262 | 17 | |
| α-helix | 268-270 | 3 | |
| β-strand | 272-273 | 2 | 5 |
| β-strand | 274-275 | 2 | 6 |
| β-strand | 276 | 1 | 7 |
| β-strand | 278 | 1 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-59 | 32 | |
| α-helix | 65-86 | 22 | |
| α-helix | 93-110 | 18 | |
| α-helix | 116-126 | 11 | |
| β-strand | 135-137 | 3 | 19 |
| β-strand | 142-148 | 7 | 19 |
| β-strand | 152-157 | 6 | 19 |
| β-strand | 162-166 | 5 | 19 |
| α-helix | 167-170 | 4 | |
| β-strand | 175-177 | 3 | 24 |
| β-strand | 183-185 | 3 | 25 |
| β-strand | 188-192 | 5 | 26 |
| α-helix | 198-211 | 14 | |
| β-strand | 215 | 1 | 25 |
| β-strand | 222-228 | 7 | 26 |
| β-strand | 233-238 | 6 | 26 |
| β-strand | 240-242 | 3 | 25 |
| α-helix | 246-262 | 17 | |
| α-helix | 268-270 | 3 | |
| β-strand | 272-273 | 2 | 22 |
| β-strand | 274-275 | 2 | 27 |
| β-strand | 276 | 1 | 23 |
| β-strand | 278-279 | 2 | 28 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-59 | 32 | |
| α-helix | 65-86 | 22 | |
| α-helix | 93-110 | 18 | |
| α-helix | 116-126 | 11 | |
| β-strand | 135-137 | 3 | 24 |
| β-strand | 142-148 | 7 | 24 |
| β-strand | 152-157 | 6 | 24 |
| β-strand | 162-166 | 5 | 24 |
| α-helix | 167-170 | 4 | |
| β-strand | 175-177 | 3 | 29 |
| β-strand | 183-185 | 3 | 30 |
| β-strand | 188-192 | 5 | 31 |
| α-helix | 198-211 | 14 | |
| β-strand | 215 | 1 | 30 |
| β-strand | 222-228 | 7 | 31 |
| β-strand | 233-238 | 6 | 31 |
| β-strand | 240-242 | 3 | 30 |
| α-helix | 246-262 | 17 | |
| α-helix | 268-270 | 3 | |
| β-strand | 272-273 | 2 | 27 |
| β-strand | 274-275 | 2 | 32 |
| β-strand | 276-277 | 2 | 28 |
| β-strand | 278-279 | 2 | 33 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-59 | 32 | |
| α-helix | 65-86 | 22 | |
| α-helix | 93-110 | 18 | |
| α-helix | 116-126 | 11 | |
| β-strand | 135-137 | 3 | 29 |
| β-strand | 142-148 | 7 | 29 |
| β-strand | 152-157 | 6 | 29 |
| β-strand | 162-166 | 5 | 29 |
| α-helix | 167-170 | 4 | |
| β-strand | 175-177 | 3 | 1 |
| β-strand | 183-185 | 3 | 34 |
| β-strand | 188-192 | 5 | 35 |
| α-helix | 198-211 | 14 | |
| β-strand | 215 | 1 | 34 |
| β-strand | 222-228 | 7 | 35 |
| β-strand | 233-238 | 6 | 35 |
| β-strand | 240-242 | 3 | 34 |
| α-helix | 246-262 | 17 | |
| α-helix | 268-270 | 3 | |
| β-strand | 272-273 | 2 | 32 |
| β-strand | 274-275 | 2 | 5 |
| β-strand | 276-277 | 2 | 33 |
| β-strand | 278 | 1 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mechanosensitive channel MscS | A, B, C, D, E, F, G | protein | 286 | Escherichia coli | P0C0S1 (AlphaFold model) |
>6VYL_1 Mechanosensitive channel MscS (chains A, B, C, D, E, F, G) MEDLNVVDSINGAGSWLVANQALLLSYAVNIVAALAIIIVGLIIARMISNAVNRLMISRK IDATVADFLSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAA GVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFSR EPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVW SNSGDLQNVYWDVLERIKREFDAAGISFPYPQMDVNFKRVKEDKAA
Visualization of the mechanosensitive ion channel MscS under membrane tension. Zhang, Y., Daday, C., Gu, R.X. et al. Nature (2021) 590:509-514. DOI 10.1038/s41586-021-03196-w · PubMed
Other PDB entries of the same protein (UniProt P0C0S1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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