Cryo-EM structure of mechanosensitive channel MscS in PC-18:1 nanodiscs. Determined by electron microscopy at 3.2 Å resolution. Released 10 Feb 2021.
Explore 6VYK in 3D Show helices and sheets RCSB PDB PDBe
6VYK contains 63 α-helices and 70 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 | 17-20 | 4 | |
| α-helix | 24-57 | 34 | |
| α-helix | 63-89 | 27 | |
| α-helix | 94-110 | 17 | |
| α-helix | 112-126 | 15 | |
| 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 | 167-171 | 5 | |
| β-strand | 175-177 | 3 | 1 |
| β-strand | 183-192 | 10 | 2 |
| α-helix | 198-211 | 14 | |
| β-strand | 215 | 1 | 2 |
| β-strand | 222-228 | 7 | 2 |
| β-strand | 233-242 | 10 | 2 |
| α-helix | 246-264 | 19 | |
| α-helix | 268-270 | 3 | |
| β-strand | 273-279 | 7 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-20 | 4 | |
| α-helix | 24-57 | 34 | |
| α-helix | 63-89 | 27 | |
| α-helix | 94-110 | 17 | |
| α-helix | 112-126 | 15 | |
| 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 | 167-171 | 5 | |
| β-strand | 176-177 | 2 | 1 |
| β-strand | 183-192 | 10 | 4 |
| α-helix | 198-211 | 14 | |
| β-strand | 215 | 1 | 4 |
| β-strand | 222-228 | 7 | 4 |
| β-strand | 233-242 | 10 | 4 |
| α-helix | 246-264 | 19 | |
| α-helix | 268-270 | 3 | |
| β-strand | 273-279 | 7 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-20 | 4 | |
| α-helix | 24-57 | 34 | |
| α-helix | 63-89 | 27 | |
| α-helix | 94-110 | 17 | |
| α-helix | 112-126 | 15 | |
| 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 | 167-171 | 5 | |
| β-strand | 175-177 | 3 | 1 |
| β-strand | 183-192 | 10 | 6 |
| α-helix | 198-211 | 14 | |
| β-strand | 215 | 1 | 6 |
| β-strand | 222-228 | 7 | 6 |
| β-strand | 233-242 | 10 | 6 |
| α-helix | 246-264 | 19 | |
| α-helix | 268-270 | 3 | |
| β-strand | 275-279 | 5 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-20 | 4 | |
| α-helix | 24-57 | 34 | |
| α-helix | 63-89 | 27 | |
| α-helix | 94-110 | 17 | |
| α-helix | 112-126 | 15 | |
| 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 | 167-171 | 5 | |
| β-strand | 175-177 | 3 | 1 |
| β-strand | 183-192 | 10 | 9 |
| α-helix | 198-211 | 14 | |
| β-strand | 215 | 1 | 9 |
| β-strand | 222-228 | 7 | 9 |
| β-strand | 233-242 | 10 | 9 |
| α-helix | 246-264 | 19 | |
| α-helix | 268-270 | 3 | |
| β-strand | 272-279 | 8 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mechanosensitive channel MscS | A, B, C, D, E, F, G | protein | 286 | Escherichia coli | P0C0S1 (AlphaFold model) |
>6VYK_1 Mechanosensitive channel MscS (chains A, B, C, D, E, F, G) MEDLNVVDSINGAGSWLVANQALLLSYAVNIVAALAIIIVGLIIARMISNAVNRLMISRK IDATVADFLSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAA GVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFSR EPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVW SNSGDLQNVYWDVLERIKREFDAAGISFPYPQMDVNFKRVKEDKAA
| ID | Name | Formula | Copies |
|---|---|---|---|
| PCW | 1,2-dioleoyl-sn-glycero-3-phosphocholine | C44 H85 N O8 P | 7 |
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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