Research workbench
AlphaFold monomer V2.0 prediction for aspartate--tRNA ligase (A6VQA9)
Analyse AlphaFold monomer V2.0 prediction for aspartate--tRNA ligase (A6VQA9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A6VQA9
- Type
- protein
- Length
- 589 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- Aspartate--tRNA ligase
- UniProt
- A6VQA9
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate--tRNA ligase | protein | 589 | 34% helix, 25% strand | A6VQA9 |
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 | 472 | 0.75 | 0.84 | 48 | empty |
| 2 | 204 | 0.46 | 0.74 | 30 | empty |
| 3 | 104 | 0.34 | 0.73 | 23 | empty |
| 4 | 54 | 0.28 | 0.75 | 14 | 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 A6VQA9
- Elsewhere: UniProt A6VQA9 · AlphaFold DB A6VQA9
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