Research workbench
AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (A3DET1)
Analyse AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (A3DET1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3DET1
- Type
- protein
- Length
- 635 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Threonine--tRNA ligase
- UniProt
- A3DET1
- Pockets
- 4 · best druggability 0.67
Structure
1 distinct chain · 39% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Threonine--tRNA ligase | protein | 635 | 39% helix, 29% strand | A3DET1 |
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 | 366 | 0.67 | 0.81 | 38 | empty |
| 2 | 140 | 0.43 | 0.75 | 21 | empty |
| 3 | 71 | 0.36 | 0.77 | 13 | empty |
| 4 | 50 | 0.27 | 0.74 | 12 | 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 A3DET1
- Elsewhere: UniProt A3DET1 · AlphaFold DB A3DET1
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