Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (B4SVG0)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (B4SVG0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B4SVG0
- Type
- protein
- Length
- 577 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x59a703CF5f3d296F946D2f7C100865462A66F361
- Molecule
- Arginine--tRNA ligase
- UniProt
- B4SVG0
- Pockets
- 8 · 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 | B4SVG0 |
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 | 369 | 0.65 | 0.79 | 40 | empty |
| 2 | 72 | 0.52 | 0.85 | 18 | empty |
| 3 | 136 | 0.48 | 0.79 | 22 | empty |
| 4 | 118 | 0.40 | 0.75 | 16 | empty |
| 5 | 63 | 0.30 | 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 B4SVG0
- Elsewhere: UniProt B4SVG0 · AlphaFold DB B4SVG0
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