Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (Q6G316)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (Q6G316) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6G316
- Type
- protein
- Length
- 585 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xab9043322A71a81ea610290ba422DBfFACaFffDf
- Molecule
- Arginine--tRNA ligase
- UniProt
- Q6G316
- Pockets
- 4 · best druggability 0.65
Structure
1 distinct chain · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 585 | 53% helix, 13% strand | Q6G316 |
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 | 400 | 0.65 | 0.78 | 48 | empty |
| 2 | 56 | 0.40 | 0.81 | 15 | empty |
| 3 | 117 | 0.38 | 0.74 | 18 | empty |
| 4 | 67 | 0.32 | 0.75 | 15 | 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 Q6G316
- Elsewhere: UniProt Q6G316 · AlphaFold DB Q6G316
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