Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (A5N8F9)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (A5N8F9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5N8F9
- Type
- protein
- Length
- 566 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc179FcAd565352aef7349a1598def4650f5E59C5
- Molecule
- Arginine--tRNA ligase
- UniProt
- A5N8F9
- Pockets
- 6 · best druggability 0.59
Structure
1 distinct chain · 59% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 566 | 59% helix, 11% strand | A5N8F9 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 304 | 0.59 | 0.77 | 46 | empty |
| 2 | 86 | 0.47 | 0.81 | 14 | empty |
| 3 | 159 | 0.45 | 0.75 | 22 | empty |
| 4 | 95 | 0.44 | 0.79 | 18 | empty |
| 5 | 84 | 0.35 | 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 A5N8F9
- Elsewhere: UniProt A5N8F9 · AlphaFold DB A5N8F9
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