Research workbench
AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (B1V8X4)
Analyse AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (B1V8X4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1V8X4
- Type
- protein
- Length
- 457 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x40B9C9d5F084D34d026E9d5Dd10501AcdF6d6152
- Molecule
- Asparagine--tRNA ligase
- UniProt
- B1V8X4
- Pockets
- 4 · best druggability 0.70
Structure
1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Asparagine--tRNA ligase | protein | 457 | 37% helix, 26% strand | B1V8X4 |
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 | 464 | 0.70 | 0.80 | 55 | empty |
| 2 | 194 | 0.53 | 0.78 | 24 | empty |
| 3 | 58 | 0.32 | 0.76 | 17 | empty |
| 4 | 58 | 0.24 | 0.72 | 14 | 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 B1V8X4
- Elsewhere: UniProt B1V8X4 · AlphaFold DB B1V8X4
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