Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (Q0AU94)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (Q0AU94) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0AU94
- Type
- protein
- Length
- 559 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Arginine--tRNA ligase
- UniProt
- Q0AU94
- Pockets
- 4 · best druggability 0.67
Structure
1 distinct chain · 55% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 559 | 55% helix, 13% strand | Q0AU94 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 533 | 0.67 | 0.78 | 64 | empty |
| 2 | 340 | 0.58 | 0.76 | 38 | empty |
| 3 | 84 | 0.33 | 0.74 | 19 | empty |
| 4 | 51 | 0.25 | 0.73 | 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 Q0AU94
- Elsewhere: UniProt Q0AU94 · AlphaFold DB Q0AU94
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