Research workbench
AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (Q0TMF3)
Analyse AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (Q0TMF3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0TMF3
- Type
- protein
- Length
- 465 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71112d4fF7ebb3b617963c05f052289e073082FD
- Molecule
- Asparagine--tRNA ligase
- UniProt
- Q0TMF3
- Pockets
- 5 · best druggability 0.68
Structure
1 distinct chain · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Asparagine--tRNA ligase | protein | 465 | 34% helix, 25% strand | Q0TMF3 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 439 | 0.68 | 0.80 | 46 | empty |
| 2 | 211 | 0.56 | 0.78 | 21 | empty |
| 3 | 90 | 0.41 | 0.78 | 20 | empty |
| 4 | 68 | 0.38 | 0.79 | 14 | empty |
| 5 | 85 | 0.30 | 0.72 | 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 Q0TMF3
- Elsewhere: UniProt Q0TMF3 · AlphaFold DB Q0TMF3
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