Research workbench
AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (Q2NU85)
Analyse AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (Q2NU85) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2NU85
- Type
- protein
- Length
- 466 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3c6e3C70425C7a2f06b2cebf5636635003E01d5F
- Molecule
- Asparagine--tRNA ligase
- UniProt
- Q2NU85
- Pockets
- 4 · best druggability 0.69
Structure
1 distinct chain · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Asparagine--tRNA ligase | protein | 466 | 32% helix, 26% strand | Q2NU85 |
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 | 447 | 0.69 | 0.81 | 54 | empty |
| 2 | 132 | 0.47 | 0.78 | 18 | empty |
| 3 | 156 | 0.44 | 0.75 | 21 | empty |
| 4 | 70 | 0.43 | 0.81 | 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 Q2NU85
- Elsewhere: UniProt Q2NU85 · AlphaFold DB Q2NU85
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