Research workbench
AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (Q5HFW9)
Analyse AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (Q5HFW9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5HFW9
- Type
- protein
- Length
- 430 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- Asparagine--tRNA ligase
- UniProt
- Q5HFW9
- Pockets
- 3 · best druggability 0.71
Structure
1 distinct chain · 34% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Asparagine--tRNA ligase | protein | 430 | 34% helix, 29% strand | Q5HFW9 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 419 | 0.71 | 0.82 | 56 | empty |
| 2 | 304 | 0.58 | 0.77 | 43 | empty |
| 3 | 104 | 0.38 | 0.75 | 19 | 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 Q5HFW9
- Elsewhere: UniProt Q5HFW9 · AlphaFold DB Q5HFW9
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