UniProt Q9Z4Z5
asparagine oxygenase (Q9Z4Z5)
asparagine oxygenase (UniProt Q9Z4Z5): 6 experimental structures and 1 predicted model on GenesisL1, 4 ligands bound, 11 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.
- UniProt
- Q9Z4Z5
- Protein
- asparagine oxygenase
- Experimental structures
- 6
- Predicted models
- 1
- Ligands
- 4
- Pockets
- 11 · 3 records with a druggable one
Structures
7 records of Q9Z4Z5 in the MolNFT archive: 6 experimental, 1 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 2OG5 | Crystal structure of asparagine oxygenase (AsnO) | x-ray diffraction | A | NA | 3 (best 0.67) |
| 2OG5 | Crystal structure of asparagine oxygenase (asno) | x-ray diffraction | A | — | — |
| 2OG6 | Crystal structure of asparagine oxygenase in complex with Fe(II) | x-ray diffraction | A | FE2, CL | 4 (best 0.67) |
| 2OG6 | Crystal structure of asparagine oxygenase in complex with FE(II) | x-ray diffraction | A | — | — |
| 2OG7 | Cystal structure of asparagine oxygenase in complex with Fe(II), 2S,3S-3-hydroxyasparagine and… | x-ray diffraction | A | FE2, AHB | 4 (best 0.73) |
| 2OG7 | Cystal structure of asparagine oxygenase in complex with FE(II), 2S, 3S-3-hydroxyasparagine and… | x-ray diffraction | A | — | — |
| Q9Z4Z5 | AlphaFold monomer V2.0 prediction for L-asparagine oxygenase (Q9Z4Z5) | predicted | A | — | — |
Ligands
Experiment against prediction
- 2OG5 chain A against the predicted model Q9Z4Z5: TM-score 0.99, RMSD 0.64 Å
- 2OG5 chain A against the predicted model Q9Z4Z5: TM-score 0.99, RMSD 0.64 Å
- 2OG6 chain A against the predicted model Q9Z4Z5: TM-score 0.99, RMSD 0.85 Å
- 2OG6 chain A against the predicted model Q9Z4Z5: TM-score 0.99, RMSD 0.85 Å
- 2OG7 chain A against the predicted model Q9Z4Z5: TM-score 0.98, RMSD 1.36 Å
- 2OG7 chain A against the predicted model Q9Z4Z5: TM-score 0.98, RMSD 1.36 Å
Elsewhere
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.