UniProt P46011
Bifunctional nitrilase/nitrile hydratase NIT4 (P46011)
Bifunctional nitrilase/nitrile hydratase NIT4 (UniProt P46011), EC 3.5.5.1, 3.5.5.4: 7 experimental structures on GenesisL1, 38 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- P46011
- Protein
- Bifunctional nitrilase/nitrile hydratase NIT4
- EC
- 3.5.5.1, 3.5.5.4, 4.2.1.65
- Experimental structures
- 7
- Predicted models
- 0
- Pockets
- 38 · 2 records with a druggable one
Structures
7 records of P46011 in the MolNFT archive: 7 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 6I00 | Cryo-EM informed directed evolution of Nitrilase 4 leads to a change in quaternary structure. | electron microscopy | J, I, H, G, F, E, D, C, B, A, L, K | — | 20 (best 0.77) |
| 6I00 | Cryo-EM informed directed evolution of nitrilase 4 leads to a change in quaternary structure. | electron microscopy | J, I, H, G, F, E, D, C, B, A, L, K | — | — |
| 6I5T | Cryo-EM informed directed evolution of Nitrilase 4 leads to a change in quaternary structure. | electron microscopy | F, E, D, C, B, A | — | — |
| 6I5T | Cryo-EM informed directed evolution of nitrilase 4 leads to a change in quaternary structure. | electron microscopy | F, E, D, C, B, A | — | — |
| 6I5U | Cryo-EM informed directed evolution of Nitrilase 4 leads to a change in quaternary structure. | electron microscopy | F, E, D, C, B, A | — | 18 (best 0.79) |
| 6I5U | Cryo-EM informed directed evolution of nitrilase 4 leads to a change in quaternary structure. | electron microscopy | F, E, D, C, B, A | — | — |
| P46011 | AlphaFold monomer V2.0 prediction for bifunctional NITRILASE/NITRILE hydratase NIT4 (P46011) | — | — | — |
Elsewhere
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