Research workbench
AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (B1YP13)
Analyse AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (B1YP13) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1YP13
- Type
- protein
- Length
- 635 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Threonine--tRNA ligase
- UniProt
- B1YP13
- Pockets
- 6 · best druggability 0.70
Structure
1 distinct chain · 40% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Threonine--tRNA ligase | protein | 635 | 40% helix, 29% strand | B1YP13 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 379 | 0.70 | 0.82 | 34 | empty |
| 2 | 173 | 0.50 | 0.77 | 28 | empty |
| 3 | 56 | 0.31 | 0.76 | 12 | empty |
| 4 | 53 | 0.30 | 0.76 | 10 | empty |
| 5 | 51 | 0.29 | 0.75 | 11 | 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 B1YP13
- Elsewhere: UniProt B1YP13 · AlphaFold DB B1YP13
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