Bacillus subtilis Ffh in complex with ppGpp. Determined by X-ray diffraction at 2.51 Å resolution. Released 2 Feb 2022.
Explore 7O9F in 3D Show helices and sheets RCSB PDB PDBe
7O9F contains 48 α-helices and 24 β-strands across 3 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 | 4-19 | 16 | |
| α-helix | 25-41 | 17 | |
| α-helix | 46-60 | 15 | |
| α-helix | 63-66 | 4 | |
| α-helix | 71-87 | 17 | |
| α-helix | 93-95 | 3 | |
| α-helix | 101 | 1 | |
| β-strand | 102-107 | 6 | 1 |
| α-helix | 114-129 | 16 | |
| β-strand | 133-138 | 6 | 1 |
| α-helix | 145-156 | 12 | |
| β-strand | 160-161 | 2 | 1 |
| α-helix | 169-183 | 15 | |
| β-strand | 187-192 | 6 | 1 |
| α-helix | 200-213 | 14 | |
| β-strand | 217-223 | 7 | 1 |
| α-helix | 224-226 | 3 | |
| α-helix | 228-240 | 13 | |
| β-strand | 245-249 | 5 | 1 |
| α-helix | 251-253 | 3 | |
| α-helix | 258-267 | 10 | |
| α-helix | 269-270 | 2 | |
| β-strand | 271-275 | 5 | 1 |
| β-strand | 283-285 | 3 | 1 |
| α-helix | 288-295 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-19 | 16 | |
| α-helix | 25-41 | 17 | |
| α-helix | 46-66 | 21 | |
| α-helix | 71-86 | 16 | |
| α-helix | 93-95 | 3 | |
| α-helix | 101 | 1 | |
| β-strand | 102-107 | 6 | 2 |
| α-helix | 114-129 | 16 | |
| β-strand | 133-137 | 5 | 2 |
| α-helix | 145-156 | 12 | |
| β-strand | 160-161 | 2 | 2 |
| α-helix | 169-182 | 14 | |
| β-strand | 187-191 | 5 | 2 |
| α-helix | 200-213 | 14 | |
| β-strand | 217-223 | 7 | 2 |
| α-helix | 224-226 | 3 | |
| α-helix | 228-240 | 13 | |
| β-strand | 245-249 | 5 | 2 |
| α-helix | 251-253 | 3 | |
| α-helix | 258-267 | 10 | |
| α-helix | 269-270 | 2 | |
| β-strand | 271-275 | 5 | 2 |
| β-strand | 283-285 | 3 | 2 |
| α-helix | 288-296 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-18 | 15 | |
| α-helix | 25-41 | 17 | |
| α-helix | 46-60 | 15 | |
| α-helix | 71-86 | 16 | |
| α-helix | 91-93 | 3 | |
| β-strand | 102-107 | 6 | 3 |
| α-helix | 114-127 | 14 | |
| β-strand | 134-136 | 3 | 3 |
| α-helix | 145-155 | 11 | |
| β-strand | 160-161 | 2 | 3 |
| α-helix | 169-181 | 13 | |
| β-strand | 187-191 | 5 | 3 |
| α-helix | 200-207 | 8 | |
| β-strand | 217-223 | 7 | 3 |
| α-helix | 224-226 | 3 | |
| α-helix | 228-240 | 13 | |
| β-strand | 245-249 | 5 | 3 |
| α-helix | 251-253 | 3 | |
| α-helix | 258-267 | 10 | |
| α-helix | 269-270 | 2 | |
| β-strand | 271-275 | 5 | 3 |
| β-strand | 283-285 | 3 | 3 |
| α-helix | 288-296 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Signal recognition particle protein | A, B, C | protein | 310 | Bacillus subtilis (strain 168) | P37105 (AlphaFold model) |
>7O9F_1 Signal recognition particle protein (chains A, B, C) MGHHHHHHMGFEGLADRLQQTISKIRGKGKVSEQDVKEMMREVRLALLEADVNFKVVKDF VKKVSERAVGQDVMKSLTPGQQVIKVVQEELTELMGGEESKIAVAKRPPTVIMMVGLQGA GKTTTSGKLANLLRKKHNRKPMLVAADIYRPAAIKQLETLGKQLDMPVFSLGDQVSPVEI AKQAIEKAKEEHYDYVILDTAGRLHIDHELMDELTNVKEIANPEEIFLVVDSMTGQDAVN VAKSFNEQLGLTGVVLTKLDGDTRGGAALSIRAVTNTPIKFAGLGEKLDALEPFHPERMA SRILGMGDLE
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 P37105 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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