Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (A5GP97)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (A5GP97) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5GP97
- Type
- protein
- Length
- 597 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3aEE739629077DbA5E2D0D9F4655D362a335420a
- Molecule
- Arginine--tRNA ligase
- UniProt
- A5GP97
- Pockets
- 8 · best druggability 0.60
Structure
1 distinct chain · 55% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 597 | 55% helix, 12% strand | A5GP97 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 249 | 0.60 | 0.80 | 34 | empty |
| 2 | 85 | 0.57 | 0.87 | 19 | empty |
| 3 | 209 | 0.48 | 0.75 | 31 | empty |
| 4 | 92 | 0.38 | 0.76 | 15 | empty |
| 5 | 75 | 0.32 | 0.74 | 25 | 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 A5GP97
- Elsewhere: UniProt A5GP97 · AlphaFold DB A5GP97
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