Research workbench
AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (A5N258)
Analyse AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (A5N258) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5N258
- Type
- protein
- Length
- 637 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xcFf9BA0aF3DBABCc89e611059882CCFef4E731f4
- Molecule
- Threonine--tRNA ligase
- UniProt
- A5N258
- Pockets
- 4 · best druggability 0.66
Structure
1 distinct chain · 39% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Threonine--tRNA ligase | protein | 637 | 39% helix, 29% strand | A5N258 |
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 | 362 | 0.66 | 0.80 | 39 | empty |
| 2 | 86 | 0.44 | 0.80 | 15 | empty |
| 3 | 146 | 0.43 | 0.75 | 25 | empty |
| 4 | 65 | 0.30 | 0.74 | 15 | 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 A5N258
- Elsewhere: UniProt A5N258 · AlphaFold DB A5N258
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