Research workbench
AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (A8LE67)
Analyse AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (A8LE67) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A8LE67
- Type
- protein
- Length
- 658 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- Threonine--tRNA ligase
- UniProt
- A8LE67
- Pockets
- 4 · best druggability 0.70
Structure
1 distinct chain · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Threonine--tRNA ligase | protein | 658 | 36% helix, 29% strand | A8LE67 |
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 | 408 | 0.70 | 0.82 | 38 | empty |
| 2 | 64 | 0.51 | 0.86 | 24 | empty |
| 3 | 107 | 0.41 | 0.77 | 20 | empty |
| 4 | 62 | 0.29 | 0.74 | 19 | 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 A8LE67
- Elsewhere: UniProt A8LE67 · AlphaFold DB A8LE67
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