UniProt Q2FUQ0
50S ribosomal protein L34 (Q2FUQ0)
50S ribosomal protein L34 (UniProt Q2FUQ0): 20 experimental structures and 1 predicted model on GenesisL1, 2 ligands bound, 5 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.
- UniProt
- Q2FUQ0
- Protein
- 50S ribosomal protein L34
- Experimental structures
- 20
- Predicted models
- 1
- Ligands
- 2
- Pockets
- 5 · 3 records with a druggable one
Structures
21 records of Q2FUQ0 in the MolNFT archive: 20 experimental, 1 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 4WCE | The crystal structure of the large ribosomal subunit of staphylococcus aureus | x-ray diffraction | 2 | — | — |
| 4WF9 | The crystal structure of the large ribosomal subunit of staphylococcus aureus in complex with… | x-ray diffraction | 2 | — | — |
| 4WFA | The crystal structure of the large ribosomal subunit of staphylococcus aureus in complex with… | x-ray diffraction | 2 | — | — |
| 4WFB | The crystal structure of the large ribosomal subunit of staphylococcus aureus in complex with… | x-ray diffraction | 2 | — | — |
| 5HKV | The crystal structure of the large ribosomal subunit of staphylococcus aureus in complex with… | x-ray diffraction | 2 | — | — |
| 5HL7 | The crystal structure of the large ribosomal subunit of staphylococcus aureus in complex with… | x-ray diffraction | 2 | — | — |
| 5LI0 | 70S ribosome from Staphylococcus aureus | electron microscopy | 6 | — | — |
| 5ND8 | Hibernating ribosome from Staphylococcus aureus (Unrotated state) | electron microscopy | 6 | — | 1 (best 0.85) |
| 5ND9 | Hibernating ribosome from Staphylococcus aureus (Rotated state) | electron microscopy | 6 | — | — |
| 5NRG | The crystal structure of the large ribosomal subunit of Staphylococcus aureus in complex with RB02 | x-ray diffraction | 2 | MN, MG | 3 (best 0.85) |
| 5NRG | The crystal structure of the large ribosomal subunit of staphylococcus aureus in complex with RB02 | x-ray diffraction | 2 | MG | — |
| 5TCU | Methicillin sensitive Staphylococcus aureus 70S ribosome | electron microscopy | LG | — | — |
| 6SJ6 | Cryo-EM structure of 50S-RsfS complex from Staphylococcus aureus | electron microscopy | 6 | — | — |
| 6SJ6 | Cryo-EM structure of 50S-rsfs complex from staphylococcus aureus | electron microscopy | 6 | — | — |
| 6YEF | 70S initiation complex with assigned rRNA modifications from Staphylococcus aureus | electron microscopy | 6 | MG | — |
| 7NHL | VgaA-LC, an antibiotic resistance ABCF, in complex with 70S ribosome from Staphylococcus aureus | electron microscopy | 7 | — | — |
| 7NHM | 70S ribosome from Staphylococcus aureus | electron microscopy | 7 | — | 1 (best 0.85) |
| 8P2F | Staphylococcus aureus 70S ribosome with elongation factor G locked with fusidic acid cyclopentane… | electron microscopy | 7 | — | — |
| 8P2G | Staphylococcus aureus 70S ribosome with elongation factor G locked with fusidic acid cyclopentane… | electron microscopy | 7 | — | — |
| 8P2H | Staphylococcus aureus 70S ribosome with elongation factor G locked with fusidic acid with a tRNA in… | electron microscopy | 7 | — | — |
| Q2FUQ0 | AlphaFold monomer V2.0 prediction for 50S ribosomal protein L34 (Q2FUQ0) | predicted | A | — | — |
Ligands
Experiment against prediction
- 8P2G chain 7 against the predicted model Q2FUQ0: TM-score 0.96, RMSD 0.40 Å
- 8P2H chain 7 against the predicted model Q2FUQ0: TM-score 0.96, RMSD 0.41 Å
- 8P2F chain 7 against the predicted model Q2FUQ0: TM-score 0.96, RMSD 0.43 Å
- 6YEF chain 6 against the predicted model Q2FUQ0: TM-score 0.95, RMSD 0.47 Å
- 5HKV chain 2 against the predicted model Q2FUQ0: TM-score 0.94, RMSD 0.52 Å
- 7NHM chain 7 against the predicted model Q2FUQ0: TM-score 0.94, RMSD 0.52 Å
- 7NHL chain 7 against the predicted model Q2FUQ0: TM-score 0.94, RMSD 0.53 Å
- 5HL7 chain 2 against the predicted model Q2FUQ0: TM-score 0.93, RMSD 0.54 Å
- 4WFA chain 2 against the predicted model Q2FUQ0: TM-score 0.93, RMSD 0.58 Å
- 4WF9 chain 2 against the predicted model Q2FUQ0: TM-score 0.93, RMSD 0.61 Å
Elsewhere
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