Research workbench
AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (A1RK52)
Analyse AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (A1RK52) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1RK52
- Type
- protein
- Length
- 466 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- Molecule
- Asparagine--tRNA ligase
- UniProt
- A1RK52
- Pockets
- 3 · best druggability 0.70
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 | A1RK52 |
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 | 512 | 0.70 | 0.80 | 60 | empty |
| 2 | 155 | 0.50 | 0.78 | 22 | empty |
| 3 | 53 | 0.27 | 0.74 | 15 | 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 A1RK52
- Elsewhere: UniProt A1RK52 · AlphaFold DB A1RK52
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