Research workbench
AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (Q2S238)
Analyse AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (Q2S238) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2S238
- Type
- protein
- Length
- 412 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Tyrosine--tRNA ligase
- UniProt
- Q2S238
- Pockets
- 4 · best druggability 0.80
Structure
1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine--tRNA ligase | protein | 412 | 51% helix, 14% strand | Q2S238 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 431 | 0.80 | 0.88 | 50 | empty |
| 2 | 55 | 0.40 | 0.80 | 11 | empty |
| 3 | 105 | 0.37 | 0.74 | 20 | empty |
| 4 | 71 | 0.32 | 0.75 | 16 | 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 Q2S238
- Elsewhere: UniProt Q2S238 · AlphaFold DB Q2S238
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