Escherichia coli FtsY in complex with pppGpp. Determined by X-ray diffraction at 2.4 Å resolution. Released 2 Feb 2022.
Explore 7O9H in 3D Show helices and sheets RCSB PDB PDBe
7O9H contains 35 α-helices and 21 β-strands across 2 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 | 196-202 | 7 | |
| α-helix | 204-207 | 4 | |
| α-helix | 211-214 | 4 | |
| α-helix | 215-218 | 4 | |
| 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 | |
| β-strand | 294-299 | 6 | 2 |
| α-helix | 306-319 | 14 | |
| β-strand | 324-329 | 6 | 2 |
| α-helix | 334-347 | 14 | |
| β-strand | 351-352 | 2 | 2 |
| α-helix | 360-373 | 14 | |
| β-strand | 378-383 | 6 | 2 |
| α-helix | 389-391 | 3 | |
| α-helix | 393-405 | 13 | |
| β-strand | 414-420 | 7 | 2 |
| α-helix | 421-423 | 3 | |
| α-helix | 426-438 | 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 | 485-493 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 196-202 | 7 | |
| α-helix | 206-208 | 3 | |
| α-helix | 211-214 | 4 | |
| α-helix | 215-218 | 4 | |
| β-strand | 222 | 1 | 3 |
| α-helix | 225-237 | 13 | |
| α-helix | 242-258 | 17 | |
| β-strand | 263 | 1 | 3 |
| α-helix | 264-266 | 3 | |
| α-helix | 267-280 | 14 | |
| β-strand | 283 | 1 | 4 |
| β-strand | 294-299 | 6 | 4 |
| α-helix | 306-319 | 14 | |
| β-strand | 324-327 | 4 | 4 |
| α-helix | 334-347 | 14 | |
| β-strand | 351-352 | 2 | 4 |
| α-helix | 360-373 | 14 | |
| β-strand | 378-381 | 4 | 4 |
| α-helix | 390-407 | 18 | |
| β-strand | 414-420 | 7 | 4 |
| α-helix | 421-423 | 3 | |
| α-helix | 425-438 | 14 | |
| β-strand | 442-446 | 5 | 4 |
| α-helix | 456-464 | 9 | |
| β-strand | 468-472 | 5 | 4 |
| α-helix | 477-479 | 3 | |
| β-strand | 480-482 | 3 | 4 |
| α-helix | 485-493 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Signal recognition particle receptor FtsY | A, B | protein | 312 | Escherichia coli DH5[alpha] | P10121 (AlphaFold model) |
>7O9H_1 Signal recognition particle receptor FtsY (chains A, B) MGGFFARLKRSLLKTKENLGSGFISLFRGKKIDDDLFEELEEQLLIADVGVETTRKIITN LTEGASRKQLRDAEALYGLLKEEMGEILAKVDEPLNVEGKTPFVILMVGVNGVGKTTTIG KLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAA KARNIDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDVEAPHEVMLTIDASTGQNAVSQA KLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEA LFAREDHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| 0O2 | guanosine 5'-(tetrahydrogen triphosphate) 3'-(trihydrogen diphosphate) | C10 H18 N5 O20 P5 | 2 |
Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp. Czech, L., Mais, C.N., Kratzat, H. et al. Nat Commun (2022) 13:1069-1069. DOI 10.1038/s41467-022-28675-0 · PubMed
Other PDB entries of the same protein (UniProt P10121 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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