UniProt A0A059VAZ3
Lon protease (A0A059VAZ3)
Lon protease (UniProt A0A059VAZ3), EC 3.4.21.53: 24 experimental structures on GenesisL1, 4 ligands bound, 121 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- A0A059VAZ3
- Protein
- Lon protease
- EC
- 3.4.21.53
- Experimental structures
- 24
- Predicted models
- 0
- Ligands
- 4
- Pockets
- 121 · 6 records with a druggable one
Structures
24 records of A0A059VAZ3 in the MolNFT archive: 24 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 4YPL | Crystal structure of a hexameric LonA protease bound to three ADPs | x-ray diffraction | A, B, C, F, D, E | — | — |
| 4YPL | Crystal structure of a hexameric lona protease bound to three adps | x-ray diffraction | A, B, C, F, D, E | — | — |
| 4YPM | Crystal structure of a LonA protease domain in complex with bortezomib | x-ray diffraction | A | — | — |
| 4YPM | Crystal structure of a lona protease domain in complex with bortezomib | x-ray diffraction | A | — | — |
| 4YPN | Crystal structure of a LonA fragment containing the 3-helix bundle and the AAA-alpha/beta domain | x-ray diffraction | A | — | — |
| 4YPN | Crystal structure of a lona fragment containing the 3-helix bundle and the aaa-ALPHA/BETA domain | x-ray diffraction | A | — | — |
| 5E7S | Hexameric structure of a LonA protease domain in active state | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L | — | — |
| 5E7S | Hexameric structure of a lona protease domain in active state | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L | — | — |
| 6WQH | Molecular basis for the ATPase-powered substrate translocation by the Lon AAA+ protease | electron microscopy | A, B, C, F, D, E | AGS, 4KZ, ADP | 20 (best 0.84) |
| 6WQH | Molecular basis for the ATPase-powered substrate translocation by the lon aaa+ protease | electron microscopy | A, B, C, F, D, E | AGS, 4KZ, ADP | — |
| 7CR9 | Crystal structure of the N-terminal fragment (residue 1-206) of lona protease from meiothermus… | x-ray diffraction | A, B | — | — |
| 7CRA | Crystal structure of the N-terminal fragment (residue 1-291) of LonA protease from Meiothermus… | x-ray diffraction | A | SO4 | 1 (best 0.28) |
| 7CRA | Crystal structure of the N-terminal fragment (residue 1-291) of lona protease from meiothermus… | x-ray diffraction | A | SO4 | — |
| 7FD4 | A complete three-dimensional structure of the lon protease translocating a protein substrate… | electron microscopy | B, C, D, E, F, A | AGS, 4KZ, ADP | — |
| 7FD5 | A complete three-dimensional structure of the lon protease translocating a protein substrate… | electron microscopy | F, B, D, C, E, A | ADP, 4KZ, AGS | — |
| 7FID | Processive cleavage of substrate at individual proteolytic active sites of the lon proteasecomplex… | electron microscopy | B, C, D, E, F, A | AGS, ADP | — |
| 7FIE | Processive cleavage of substrate at individual proteolytic active sites of the lon protease complex… | electron microscopy | B, C, D, E, F, A | AGS, ADP | — |
| 7FIZ | Processive cleavage of substrate at individual proteolytic active sites of the lon protease complex… | electron microscopy | B, C, D, E, F, A | AGS, ADP | — |
| 7YPH | Open-spiral pentamer of the substrate-free Lon protease with a Y224S mutation | electron microscopy | A, B, C, D, E | AGS | 20 (best 0.84) |
| 7YPI | Spiral hexamer of the substrate-free Lon protease with a Y224S mutation | electron microscopy | A, B, C, D, E, F | AGS | 20 (best 0.81) |
| 7YUH | MtaLon-Apo for the spiral oligomers of trimer | electron microscopy | A, B, C | — | 20 (best 0.77) |
| 7YUT | MtaLon-Apo for the spiral oligomers of hexamer | electron microscopy | A, C, E, D, F, B | — | — |
| 7YUU | MtaLon-ADP for the spiral oligomers of trimer | electron microscopy | A, B, C | — | 20 (best 0.83) |
| 7YUX | MtaLon-ADP for the spiral oligomers of hexamer | electron microscopy | A, C, E, D, F, B | ADP | 20 (best 0.80) |
Ligands
Elsewhere
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