Research workbench
AlphaFold monomer V2.0 prediction for proline--tRNA ligase (A1V0N6)
Analyse AlphaFold monomer V2.0 prediction for proline--tRNA ligase (A1V0N6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1V0N6
- Type
- protein
- Length
- 578 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- Molecule
- Proline--tRNA ligase
- UniProt
- A1V0N6
- Pockets
- 3 · best druggability 0.70
Structure
1 distinct chain · 30% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline--tRNA ligase | protein | 578 | 30% helix, 30% strand | A1V0N6 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 481 | 0.70 | 0.81 | 48 | empty |
| 2 | 103 | 0.45 | 0.79 | 23 | empty |
| 3 | 114 | 0.39 | 0.75 | 23 | 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 A1V0N6
- Elsewhere: UniProt A1V0N6 · AlphaFold DB A1V0N6
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