UniProt A0A5W0I7H9
Flagellar motor switch protein FliG (A0A5W0I7H9)
Flagellar motor switch protein FliG (UniProt A0A5W0I7H9): 4 experimental structures on GenesisL1, 39 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- A0A5W0I7H9
- Protein
- Flagellar motor switch protein FliG
- Experimental structures
- 4
- Predicted models
- 0
- Pockets
- 39 · 4 records with a druggable one
Structures
4 records of A0A5W0I7H9 in the MolNFT archive: 4 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 8VIB | CW Flagellar Switch Complex - FliF, FliG, FliM, and FliN forming single subunit of the C-ring from… | electron microscopy | G | — | 3 (best 0.64) |
| 8VID | CW Flagellar Switch Complex with extra density - FliF, FliG, FliM, and FliN forming single subunit… | electron microscopy | G | — | 5 (best 0.79) |
| 8VKQ | CW Flagellar Switch Complex - FliF, FliG, FliM, and FliN forming the C-ring from Salmonella | electron microscopy | G, B, J, T, AA, GA, MA, SA, YA, EB, KB, QB, WB, CC, IC, OC, UC, AD, GD, MD, SD, YD, EE, KE, QE, WE, CF, IF, OF, UF, AG, GG, MG, SG | — | 16 (best 0.80) |
| 8VKR | CW Flagellar Switch Complex with extra density - FliF, FliG, FliM, and FliN forming the C-ring from… | electron microscopy | G, B, J, T, AA, GA, MA, SA, YA, EB, KB, QB, WB, CC, IC, OC, UC, AD, GD, MD, SD, YD, EE, KE, QE, WE, CF, IF, OF, UF, AG, GG, MG, SG | — | 15 (best 0.80) |
Elsewhere
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