Research workbench
AlphaFold monomer V2.0 prediction for glutamine--tRNA ligase (B5YQM4)
Analyse AlphaFold monomer V2.0 prediction for glutamine--tRNA ligase (B5YQM4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5YQM4
- Type
- protein
- Length
- 554 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x239f46D6762da5B7b108949c2F4580f21ccD7e24
- Molecule
- Glutamine--tRNA ligase
- UniProt
- B5YQM4
- Pockets
- 4 · best druggability 0.67
Structure
1 distinct chain · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine--tRNA ligase | protein | 554 | 32% helix, 25% strand | B5YQM4 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 348 | 0.67 | 0.81 | 30 | empty |
| 2 | 181 | 0.58 | 0.81 | 29 | empty |
| 3 | 130 | 0.58 | 0.84 | 20 | empty |
| 4 | 121 | 0.39 | 0.75 | 27 | 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 B5YQM4
- Elsewhere: UniProt B5YQM4 · AlphaFold DB B5YQM4
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