UniProt A0A8H6C337
60S ribosomal protein L8 (A0A8H6C337)
60S ribosomal protein L8 (UniProt A0A8H6C337): 10 experimental structures on GenesisL1, 1 ligand bound, 15 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- A0A8H6C337
- Protein
- 60S ribosomal protein L8
- Experimental structures
- 10
- Predicted models
- 0
- Ligands
- 1
- Pockets
- 15 · 9 records with a druggable one
Structures
10 records of A0A8H6C337 in the MolNFT archive: 10 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 8C3A | Crystal structure of ailanthone bound to the Candida albicans 80S ribosome | x-ray diffraction | p, BC | — | 1 (best 0.88) |
| 8CQ7 | Crystal structure of phyllanthoside bound to the Candida albicans 80S ribosome | x-ray diffraction | p, BC | — | 3 (best 0.89) |
| 8CQW | Crystal structure of the Candida albicans 80S ribosome in complex with Hygromycin B | x-ray diffraction | p, BC | — | 2 (best 0.90) |
| 8CRE | Crystal structure of the Candida albicans 80S ribosome in complex with geneticin G418 | x-ray diffraction | p, BC | — | 1 (best 0.90) |
| 8OEQ | Crystal structure of the Candida albicans 80S ribosome in complex with Paromomycin (250uM) | x-ray diffraction | p, BC | MG | 2 (best 0.89) |
| 8OGJ | Structure of Candida albicans 80S ribosome in complex with mefloquine | electron microscopy | p | — | 3 (best 0.89) |
| 8OH6 | Crystal structure of the Candida albicans 80S ribosome in complex with Paromomycin (500umol) | x-ray diffraction | p, BC | MG | 1 (best 0.90) |
| 8OI5 | Crystal structure of the Candida albicans 80S ribosome in complex with Paromomycin (2mM) | x-ray diffraction | p, BC | MG | 1 (best 0.89) |
| 8OJ3 | Crystal structure of the Candida albicans 80S ribosome in complex with geneticin G418 (rotated… | x-ray diffraction | p, BC | MG | — |
| 8Q5I | Structure of Candida albicans 80S ribosome in complex with cephaeline | electron microscopy | p | — | 1 (best 0.86) |
Ligands
- MG · Magnesium ion · in 4 records
Elsewhere
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