Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (A6SU56)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (A6SU56) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A6SU56
- Type
- protein
- Length
- 577 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- Molecule
- Arginine--tRNA ligase
- UniProt
- A6SU56
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 577 | 50% helix, 14% strand | A6SU56 |
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 | 430 | 0.64 | 0.78 | 50 | empty |
| 2 | 228 | 0.58 | 0.79 | 34 | empty |
| 3 | 74 | 0.38 | 0.78 | 18 | empty |
| 4 | 62 | 0.31 | 0.75 | 16 | 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 A6SU56
- Elsewhere: UniProt A6SU56 · AlphaFold DB A6SU56
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