UniProt Q5SIT6
V-type ATP synthase subunit I (Q5SIT6)
V-type ATP synthase subunit I (UniProt Q5SIT6): 13 experimental structures on GenesisL1, 4 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- Q5SIT6
- Protein
- V-type ATP synthase subunit I
- Experimental structures
- 13
- Predicted models
- 0
- Pockets
- 4 · 2 records with a druggable one
Structures
13 records of Q5SIT6 in the MolNFT archive: 13 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 5Y5X | V/A-type ATPASE/SYNTHASE from thermus thermophilus, rotational state 1 | electron microscopy | N | — | — |
| 5Y5Z | V/A-type ATPase/synthase from Thermus thermophilus, rotational state 2 | electron microscopy | N | — | — |
| 5Y5Z | V/A-type ATPASE/SYNTHASE from thermus thermophilus, rotational state 2 | electron microscopy | N | — | — |
| 5Y60 | V/A-type ATPase/synthase from Thermus thermophilus, rotational state 3. | electron microscopy | N | — | — |
| 5Y60 | V/A-type ATPASE/SYNTHASE from thermus thermophilus, rotational state 3. | electron microscopy | N | — | — |
| 6LY9 | The membrane-embedded vo domain of V/A-ATPase from thermus thermophilus | electron microscopy | N | — | — |
| 6QUM | Thermus thermophilus V/A-type ATPASE/SYNTHASE, rotational state 1 | electron microscopy | N | — | — |
| 6R0W | Thermus thermophilus V/A-type ATPase/synthase, rotational state 2 | electron microscopy | N | — | 2 (best 0.78) |
| 6R0W | Thermus thermophilus V/A-type ATPASE/SYNTHASE, rotational state 2 | electron microscopy | N | — | — |
| 6R0Y | Thermus thermophilus V/A-type ATPase/synthase, rotational state 3 | electron microscopy | N | — | 2 (best 0.80) |
| 6R0Y | Thermus thermophilus V/A-type ATPASE/SYNTHASE, rotational state 3 | electron microscopy | N | — | — |
| 6R0Z | Thermus thermophilus V/A-type ATPASE/SYNTHASE, rotational state 1L | electron microscopy | N | — | — |
| 6R10 | Thermus thermophilus V/A-type ATPASE/SYNTHASE, rotational state 1R | electron microscopy | N | — | — |
Elsewhere
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