UniProt Q5NGQ3
Q5NGQ3
Q5NGQ3 (UniProt Q5NGQ3): 10 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- Q5NGQ3
- Experimental structures
- 10
- Predicted models
- 0
Structures
10 records of Q5NGQ3 in the MolNFT archive: 10 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 3NRC | Crystal Structure of the Francisella tularensis enoyl-acyl carrier protein reductase (FabI) in… | x-ray diffraction | A, B | — | — |
| 3NRC | Crystal structure of the francisella tularensis enoyl-acyl carrier protein reductase (fabi) in… | x-ray diffraction | A, B | — | — |
| 3UIC | Crystal Structure of FabI, an Enoyl Reductase from F. tularensis, in complex with a Novel and… | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P | — | — |
| 3UIC | Crystal structure of fabi, an enoyl reductase from F. tularensis, in complex with a novel and… | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P | — | — |
| 4J1N | Crystal structures of FabI from F. tularensis in complex with novel inhibitors based on the… | x-ray diffraction | A, B | — | — |
| 4J1N | Crystal structures of fabi from F. tularensis in complex with novel inhibitors based on the… | x-ray diffraction | A, B | — | — |
| 4J3F | Crystal Structure of FabI from F. tularensis in complex with novel inhibitors based on the… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 4J3F | Crystal structure of fabi from F. tularensis in complex with novel inhibitors based on the… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 4J4T | Crystal Structure of FabI from F. tularensis in complex with novel inhibitors based on the… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 4J4T | Crystal structure of fabi from F. tularensis in complex with novel inhibitors based on the… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
Elsewhere
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.