YnaI in an open-like conformation. Determined by electron microscopy at 4.1 Å resolution. Released 25 Nov 2020.
Explore 6ZYE in 3D Show helices and sheets RCSB PDB PDBe
6ZYE contains 56 α-helices and 84 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 | -34--17 | 18 | |
| α-helix | 150-159 | 10 | |
| α-helix | 161-175 | 15 | |
| β-strand | 184-186 | 3 | 1 |
| β-strand | 193-198 | 6 | 1 |
| β-strand | 203-208 | 6 | 1 |
| β-strand | 213-217 | 5 | 1 |
| α-helix | 218-223 | 6 | |
| β-strand | 226-227 | 2 | 1 |
| α-helix | 229-231 | 3 | |
| β-strand | 235-243 | 9 | 5 |
| α-helix | 245-250 | 6 | |
| α-helix | 251-263 | 13 | |
| β-strand | 268 | 1 | 5 |
| β-strand | 274-275 | 2 | 5 |
| β-strand | 278-282 | 5 | 5 |
| β-strand | 285-294 | 10 | 5 |
| α-helix | 299-320 | 22 | |
| β-strand | 324 | 1 | 5 |
| β-strand | 328-332 | 5 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| YnaI,Low conductance mechanosensitive channel YnaI | A, B, C, D, E, F, G | protein | 387 | Escherichia coli (strain K12) | P0AEB5 (AlphaFold model) |
>6ZYE_1 YnaI,Low conductance mechanosensitive channel YnaI (chains A, B, C, D, E, F, G) XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXMIAELFTNNALNLVIIFGSCAALI LMSFWFRRGNRKRKGFLFHAVQFLIYTIIISAVGSIINYVIENYKLKFITPGVIDFICTS LIAVILTIKLFLLINQFEKQQIKKGRDITSARIMSRIIKITIIVVLVLLYGEHFGMSLSG LLTFGGIGGLAVGMAGKDILSNFFSGIMLYFDRPFSIGDWIRSPDRNIEGTVAEIGWRIT KITTFDNRPLYVPNSLFSSISVENPGRMTNRRITTTIGLRYEDAAKVGVIVEAVREMLKN HPAIDQRQTLLVYFNQFADSSLNIMVYCFTKTTVWAEWLAAQQDVYLKIIDIVQSHGADF AFPSQTLYMDNITPPEQGRLEHHHHHH
The MscS-like channel YnaI has a gating mechanism based on flexible pore helices. Flegler, V.J., Rasmussen, A., Rao, S. et al. Proc Natl Acad Sci U S A (2020) 117:28754-28762. DOI 10.1073/pnas.2005641117 · 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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