Research workbench
AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (A9IVB0)
Analyse AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (A9IVB0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9IVB0
- Type
- protein
- Length
- 658 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- Threonine--tRNA ligase
- UniProt
- A9IVB0
- Pockets
- 4 · best druggability 0.68
Structure
1 distinct chain · 39% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Threonine--tRNA ligase | protein | 658 | 39% helix, 28% strand | A9IVB0 |
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 | 497 | 0.68 | 0.79 | 41 | empty |
| 2 | 238 | 0.53 | 0.76 | 27 | empty |
| 3 | 62 | 0.30 | 0.75 | 16 | 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 A9IVB0
- Elsewhere: UniProt A9IVB0 · AlphaFold DB A9IVB0
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