Escherichia coli Ffh in complex with ppGpp. Determined by X-ray diffraction at 2.8 Å resolution. Released 2 Feb 2022.
Explore 7O9G in 3D Show helices and sheets RCSB PDB PDBe
7O9G contains 14 α-helices and 8 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 | 4-18 | 15 | |
| α-helix | 24-40 | 17 | |
| α-helix | 45-58 | 14 | |
| α-helix | 61-65 | 5 | |
| α-helix | 70-86 | 17 | |
| β-strand | 101-106 | 6 | 1 |
| α-helix | 113-128 | 16 | |
| β-strand | 132-136 | 5 | 1 |
| α-helix | 142-155 | 14 | |
| β-strand | 158-160 | 3 | 1 |
| α-helix | 168-181 | 14 | |
| β-strand | 186-190 | 5 | 1 |
| α-helix | 199-212 | 14 | |
| β-strand | 216-222 | 7 | 1 |
| α-helix | 223-225 | 3 | |
| α-helix | 227-239 | 13 | |
| β-strand | 244-248 | 5 | 1 |
| α-helix | 250-253 | 4 | |
| α-helix | 258-266 | 9 | |
| β-strand | 270-274 | 5 | 1 |
| β-strand | 282-284 | 3 | 1 |
| α-helix | 287-295 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Signal recognition particle protein | A | protein | 306 | Escherichia coli | P0AGD7 (AlphaFold model) |
>7O9G_1 Signal recognition particle protein (chains A) MGFDNLTDRLSRTLRNISGRGRLTEDNVKDTLREVRMALLEADVALPVVREFINRVKEKA VGHEVNKSLTPGQEFVKIVRNELVAAMGEENQTLNLAAQPPAVVLMAGLQGAGKTTSVGK LGKFLREKHKKKVLVVSADVYRPAAIKQLETLAEQVGVDFFPSDVGQKPVDIVNAALKEA KLKFYDVLLVDTAGRLHVDEAMMDEIKQVHASINPVETLFVVDAMTGQDAANTAKAFNEA LPLTGVVLTKVDGDARGGAALSIRHITGKPIKFLGVGEKTEALEPFHPDRIASRILGMGD HHHHHH
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 P0AGD7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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