Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (Q5SM45)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (Q5SM45) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5SM45
- Type
- protein
- Length
- 592 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEbf4d45776C392B0bE6c7338e714387D7664f38C
- Molecule
- Arginine--tRNA ligase
- UniProt
- Q5SM45
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 592 | 49% helix, 14% strand | Q5SM45 |
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 | 673 | 0.71 | 0.78 | 58 | empty |
| 2 | 88 | 0.34 | 0.75 | 14 | empty |
| 3 | 85 | 0.31 | 0.73 | 15 | empty |
| 4 | 58 | 0.29 | 0.74 | 18 | 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 Q5SM45
- Elsewhere: UniProt Q5SM45 · AlphaFold DB Q5SM45
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