Cryo-EM structure of MscS channel, YnaI. Determined by electron microscopy at 3.8 Å resolution. Released 20 Mar 2019.
Explore 5Y4O in 3D Show helices and sheets RCSB PDB PDBe
5Y4O contains 56 α-helices and 96 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 | 115-137 | 23 | |
| α-helix | 142-144 | 3 | |
| α-helix | 145-175 | 31 | |
| β-strand | 184 | 1 | 1 |
| β-strand | 195 | 1 | 1 |
| β-strand | 196-199 | 4 | 2 |
| β-strand | 204-206 | 3 | 2 |
| β-strand | 207 | 1 | 3 |
| β-strand | 213 | 1 | 3 |
| α-helix | 218-222 | 5 | |
| α-helix | 229-231 | 3 | |
| β-strand | 235-238 | 4 | 4 |
| β-strand | 243 | 1 | 5 |
| α-helix | 245-250 | 6 | |
| α-helix | 251-264 | 14 | |
| β-strand | 268 | 1 | 4 |
| β-strand | 274-277 | 4 | 4 |
| β-strand | 289-294 | 6 | 4 |
| α-helix | 299-319 | 21 | |
| β-strand | 324 | 1 | 5 |
| β-strand | 328 | 1 | 6 |
| β-strand | 330 | 1 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 115-137 | 23 | |
| α-helix | 142-144 | 3 | |
| α-helix | 145-175 | 31 | |
| β-strand | 184 | 1 | 26 |
| β-strand | 195 | 1 | 26 |
| β-strand | 196-199 | 4 | 27 |
| β-strand | 204-206 | 3 | 27 |
| β-strand | 207 | 1 | 28 |
| β-strand | 213 | 1 | 28 |
| α-helix | 218-222 | 5 | |
| α-helix | 229-231 | 3 | |
| β-strand | 235-238 | 4 | 29 |
| β-strand | 243 | 1 | 30 |
| α-helix | 245-250 | 6 | |
| α-helix | 251-264 | 14 | |
| β-strand | 268 | 1 | 29 |
| β-strand | 274-277 | 4 | 29 |
| β-strand | 289-294 | 6 | 29 |
| α-helix | 299-319 | 21 | |
| β-strand | 324 | 1 | 30 |
| β-strand | 328 | 1 | 25 |
| β-strand | 330-331 | 2 | 31 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 115-137 | 23 | |
| α-helix | 142-144 | 3 | |
| α-helix | 145-175 | 31 | |
| β-strand | 184 | 1 | 32 |
| β-strand | 195 | 1 | 32 |
| β-strand | 196-199 | 4 | 33 |
| β-strand | 204-206 | 3 | 33 |
| β-strand | 207 | 1 | 34 |
| β-strand | 213 | 1 | 34 |
| α-helix | 218-222 | 5 | |
| α-helix | 229-231 | 3 | |
| β-strand | 235-238 | 4 | 35 |
| β-strand | 243 | 1 | 36 |
| α-helix | 245-250 | 6 | |
| α-helix | 251-264 | 14 | |
| β-strand | 268 | 1 | 35 |
| β-strand | 274-277 | 4 | 35 |
| β-strand | 289-294 | 6 | 35 |
| α-helix | 299-319 | 21 | |
| β-strand | 324 | 1 | 36 |
| β-strand | 328-329 | 2 | 31 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 115-137 | 23 | |
| α-helix | 142-144 | 3 | |
| α-helix | 145-175 | 31 | |
| β-strand | 184 | 1 | 37 |
| β-strand | 195 | 1 | 37 |
| β-strand | 196-199 | 4 | 38 |
| β-strand | 204-206 | 3 | 38 |
| β-strand | 207 | 1 | 39 |
| β-strand | 213 | 1 | 39 |
| α-helix | 218-222 | 5 | |
| α-helix | 229-231 | 3 | |
| β-strand | 235-238 | 4 | 40 |
| β-strand | 243 | 1 | 41 |
| α-helix | 245-250 | 6 | |
| α-helix | 251-264 | 14 | |
| β-strand | 268 | 1 | 40 |
| β-strand | 274-277 | 4 | 40 |
| β-strand | 289-294 | 6 | 40 |
| α-helix | 299-319 | 21 | |
| β-strand | 324 | 1 | 41 |
| β-strand | 330 | 1 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Low conductance mechanosensitive channel YnaI | A, B, C, D, E, F, G | protein | 349 | Escherichia coli O157:H7 | P0AEB5 (AlphaFold model) |
>5Y4O_1 Low conductance mechanosensitive channel YnaI (chains A, B, C, D, E, F, G) MIAELFTNNALNLVIIFGSCAALILMSFWFRRGNRKRKGFLFHAVQFLIYTIIISAVGSI INYVIENYKLKFITPGVIDFICTSLIAVILTIKLFLLINQFEKQQIKKGRDITSARIMSR IIKITIIVVLVLLYGEHFGMSLSGLLTFGGIGGLAVGMAGKDILSNFFSGIMLYFDRPFS IGDWIRSPDRNIEGTVAEIGWRITKITTFDNRPLYVPNSLFSSISVENPGRMTNRRITTT IGLRYEDAAKVGVIVEAVREMLKNHPAIDQRQTLLVYFNQFADSSLNIMVYCFTKTTVWA EWLAAQQDVYLKIIDIVQSHGADFAFPSQTLYMDNITPPEQGRHHHHHH
A binding-block ion selective mechanism revealed by a Na/K selective channel. Yu, J., Zhang, B., Zhang, Y. et al. Protein Cell (2018) 9:629-639. DOI 10.1007/s13238-017-0465-8 · PubMed
Other PDB entries of the same protein (UniProt P0AEB5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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