Research workbench
AlphaFold monomer V2.0 prediction for glutamine--tRNA ligase (B1X6L3)
Analyse AlphaFold monomer V2.0 prediction for glutamine--tRNA ligase (B1X6L3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1X6L3
- Type
- protein
- Length
- 554 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Glutamine--tRNA ligase
- UniProt
- B1X6L3
- Pockets
- 4 · best druggability 0.65
Structure
1 distinct chain · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine--tRNA ligase | protein | 554 | 31% helix, 25% strand | B1X6L3 |
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 | 314 | 0.65 | 0.81 | 35 | empty |
| 2 | 225 | 0.61 | 0.81 | 42 | empty |
| 3 | 195 | 0.56 | 0.80 | 22 | empty |
| 4 | 114 | 0.38 | 0.75 | 24 | 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 B1X6L3
- Elsewhere: UniProt B1X6L3 · AlphaFold DB B1X6L3
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