Research workbench
AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (B3H198)
Analyse AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (B3H198) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B3H198
- Type
- protein
- Length
- 467 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x90102B4C62981b371548D152803E04D214105389
- Molecule
- Asparagine--tRNA ligase
- UniProt
- B3H198
- Pockets
- 4 · best druggability 0.69
Structure
1 distinct chain · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Asparagine--tRNA ligase | protein | 467 | 34% helix, 25% strand | B3H198 |
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 | 443 | 0.69 | 0.81 | 52 | empty |
| 2 | 108 | 0.49 | 0.81 | 15 | empty |
| 3 | 154 | 0.47 | 0.77 | 23 | empty |
| 4 | 58 | 0.27 | 0.73 | 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 B3H198
- Elsewhere: UniProt B3H198 · AlphaFold DB B3H198
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.