Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (B1L826)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (B1L826) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1L826
- Type
- protein
- Length
- 546 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- Arginine--tRNA ligase
- UniProt
- B1L826
- Pockets
- 4 · best druggability 0.61
Structure
1 distinct chain · 54% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 546 | 54% helix, 14% strand | B1L826 |
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 | 333 | 0.61 | 0.78 | 33 | empty |
| 2 | 172 | 0.47 | 0.76 | 23 | empty |
| 3 | 125 | 0.41 | 0.75 | 22 | empty |
| 4 | 56 | 0.29 | 0.75 | 12 | 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 B1L826
- Elsewhere: UniProt B1L826 · AlphaFold DB B1L826
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