Structure of the NG+1 construct of the E. coli SRP receptor FtsY. Determined by X-ray diffraction at 1.9 Å resolution. Released 2 Oct 2007.
Explore 2QY9 in 3D Show helices and sheets RCSB PDB PDBe
2QY9 contains 18 α-helices and 10 β-strands across 1 chain. 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 | 197-202 | 6 | |
| α-helix | 213-218 | 6 | |
| β-strand | 222 | 1 | 1 |
| α-helix | 225-237 | 13 | |
| α-helix | 242-258 | 17 | |
| β-strand | 263 | 1 | 1 |
| α-helix | 264-266 | 3 | |
| α-helix | 267-280 | 14 | |
| α-helix | 284-286 | 3 | |
| β-strand | 294-299 | 6 | 2 |
| α-helix | 306-318 | 13 | |
| β-strand | 324-327 | 4 | 2 |
| α-helix | 334-346 | 13 | |
| β-strand | 351-352 | 2 | 2 |
| α-helix | 360-373 | 14 | |
| β-strand | 378-381 | 4 | 2 |
| α-helix | 387-389 | 3 | |
| α-helix | 390-404 | 15 | |
| β-strand | 414-420 | 7 | 2 |
| α-helix | 421-423 | 3 | |
| α-helix | 425-437 | 13 | |
| β-strand | 442-446 | 5 | 2 |
| α-helix | 456-464 | 9 | |
| β-strand | 468-472 | 5 | 2 |
| α-helix | 477-479 | 3 | |
| β-strand | 480-482 | 3 | 2 |
| α-helix | 483 | 1 | |
| α-helix | 485-493 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cell division protein ftsY | A | protein | 309 | Escherichia coli | P10121 (AlphaFold model) |
>2QY9_1 Cell division protein ftsY (chains A) MFARLKRSLLKTKENLGSGFISLFRGKKIDDDLFEELEEQLLIADVGVETTRKIITNLTE GASRKQLRDAEALYGLLKEEMGEILAKVDEPLNVEGKAPFVILMVGVNGVGKTTTIGKLA RQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKAR NIDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDVEAPHEVMLTIDASTGQNAVSQAKLF HEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEALFA REDHHHHHH
The E. coli SRP-receptor FTSY contains an essential and autonomous membrane-binding amphipathic helix. Parlitz, R., Bange, G., Wild, K. et al. To be published.
Other PDB entries of the same protein (UniProt P10121 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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