Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (A8AFG5)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (A8AFG5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A8AFG5
- Type
- protein
- Length
- 577 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- Arginine--tRNA ligase
- UniProt
- A8AFG5
- Pockets
- 6 · best druggability 0.65
Structure
1 distinct chain · 55% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 577 | 55% helix, 12% strand | A8AFG5 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 368 | 0.65 | 0.80 | 42 | empty |
| 2 | 75 | 0.52 | 0.85 | 18 | empty |
| 3 | 127 | 0.46 | 0.78 | 21 | empty |
| 4 | 91 | 0.38 | 0.76 | 14 | empty |
| 5 | 89 | 0.32 | 0.73 | 17 | 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 A8AFG5
- Elsewhere: UniProt A8AFG5 · AlphaFold DB A8AFG5
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