UniProt A0A822U1Y5
Nucleoside triphosphate hydrolase (A0A822U1Y5)
Nucleoside triphosphate hydrolase (UniProt A0A822U1Y5): 6 experimental structures on GenesisL1, 3 ligands bound, 74 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- A0A822U1Y5
- Protein
- Nucleoside triphosphate hydrolase
- Experimental structures
- 6
- Predicted models
- 0
- Ligands
- 3
- Pockets
- 74 · 6 records with a druggable one
Structures
6 records of A0A822U1Y5 in the MolNFT archive: 6 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 8J4U | Structure of HerA-Sir2 complex from Escherichia coli Nezha system | electron microscopy | M, N, O, P, Q, R | AGS, MG | 14 (best 0.88) |
| 8SU9 | E. coli SIR2-HerA complex (hexamer HerA bound with dodecamer Sir2) | electron microscopy | M, N, O, P, Q, R | ADP, MG | 14 (best 0.89) |
| 8SUB | E. coli SIR2-HerA complex (dodecamer SIR2 pentamer HerA) | electron microscopy | M, N, O, P, Q | ADP, MG | 13 (best 0.89) |
| 8SUW | E. coli SIR2-HerA complex (dodecamer SIR2 bound 4 protomers of HerA) | electron microscopy | M, N, O, P | ADP, MG | 12 (best 0.89) |
| 8UAE | E. coli Sir2_HerA complex (12:6) with ATPgamaS | electron microscopy | M, N, O, P, Q, R | AGS, MG | 11 (best 0.89) |
| 8UAF | E. coli Sir2_HerA complex (12:6) bound with NAD+ | electron microscopy | M, N, O, P, Q, R | ADP, MG | 10 (best 0.88) |
Ligands
Elsewhere
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