UniProt P80341
50S ribosomal protein L35 (P80341)
50S ribosomal protein L35 (UniProt P80341): 10 experimental structures on GenesisL1, 1 ligand bound, 13 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- P80341
- Protein
- 50S ribosomal protein L35
- Experimental structures
- 10
- Predicted models
- 0
- Ligands
- 1
- Pockets
- 13 · 3 records with a druggable one
Structures
10 records of P80341 in the MolNFT archive: 10 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 4V4X | Crystal structure of the 70S Thermus thermophilus ribosome showing how the 16S 3'-end mimicks mRNA… | x-ray diffraction | B7 | — | — |
| 4V4Y | Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated… | x-ray diffraction | B7 | — | — |
| 4V4Z | 70S Thermus thermophilous ribosome functional complex with mRNA and E- and P-site tRNAs at 4.5A. | x-ray diffraction | B7 | — | — |
| 4V51 | Structure of the Thermus thermophilus 70S ribosome complexed with mRNA, tRNA and paromomycin | x-ray diffraction | B8, D8 | — | — |
| 4V5A | Structure of the Ribosome Recycling Factor bound to the Thermus thermophilus 70S ribosome with… | x-ray diffraction | B8, D8 | — | — |
| 4V68 | T. thermophilus 70S ribosome in complex with mRNA, tRNAs and EF-Tu.GDP.kirromycin ternary complex… | electron microscopy | B8 | — | — |
| 5WIS | Crystal structure of the Thermus thermophilus 70S ribosome in complex with methymycin and bound to… | x-ray diffraction | 18, 28 | MG | 3 (best 0.89) |
| 6CFK | Crystal structure of the Thermus thermophilus 70S ribosome in complex with D-histidyl-CAM and bound… | x-ray diffraction | 18, 28 | MG | 5 (best 0.89) |
| 6CFL | Crystal structure of the Thermus thermophilus 70S ribosome in complex with lysyl-CAM and bound to… | x-ray diffraction | 18, 28 | MG | 5 (best 0.89) |
| P80341 | AlphaFold monomer V2.0 prediction for 50S ribosomal protein L35 (P80341) | — | — | — |
Ligands
- MG · Magnesium ion · in 3 records
Elsewhere
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