Research workbench
AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (B9LCU8)
Analyse AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (B9LCU8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B9LCU8
- Type
- protein
- Length
- 440 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7827f7B56a7c719b0EaeD83AF7DF9251AC6C0C19
- Molecule
- Asparagine--tRNA ligase
- UniProt
- B9LCU8
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Asparagine--tRNA ligase | protein | 440 | 34% helix, 27% strand | B9LCU8 |
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 | 426 | 0.71 | 0.82 | 59 | empty |
| 2 | 129 | 0.44 | 0.76 | 22 | empty |
| 3 | 113 | 0.40 | 0.76 | 25 | empty |
| 4 | 54 | 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 B9LCU8
- Elsewhere: UniProt B9LCU8 · AlphaFold DB B9LCU8
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