Research workbench
AlphaFold monomer V2.0 prediction for valine--tRNA ligase (A5V592)
Analyse AlphaFold monomer V2.0 prediction for valine--tRNA ligase (A5V592) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5V592
- Type
- protein
- Length
- 896 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF798f308FcD2a0138Cc80431D1879348A6451653
- Molecule
- Valine--tRNA ligase
- UniProt
- A5V592
- Pockets
- 7 · best druggability 0.75
Structure
1 distinct chain · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Valine--tRNA ligase | protein | 896 | 48% helix, 18% strand | A5V592 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 702 | 0.75 | 0.80 | 56 | empty |
| 2 | 241 | 0.66 | 0.83 | 28 | empty |
| 3 | 356 | 0.64 | 0.79 | 43 | empty |
| 4 | 53 | 0.44 | 0.84 | 15 | empty |
| 5 | 100 | 0.43 | 0.78 | 15 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A5V592
- Elsewhere: UniProt A5V592 · AlphaFold DB A5V592
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