Research workbench
AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (Q0SVA4)
Analyse AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (Q0SVA4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0SVA4
- Type
- protein
- Length
- 406 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
- Molecule
- Tyrosine--tRNA ligase
- UniProt
- Q0SVA4
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine--tRNA ligase | protein | 406 | 49% helix, 16% strand | Q0SVA4 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 454 | 0.76 | 0.85 | 56 | empty |
| 2 | 363 | 0.60 | 0.77 | 45 | empty |
| 3 | 52 | 0.44 | 0.84 | 15 | empty |
| 4 | 89 | 0.40 | 0.77 | 13 | 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 Q0SVA4
- Elsewhere: UniProt Q0SVA4 · AlphaFold DB Q0SVA4
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