Research workbench
AlphaFold monomer V2.0 prediction for proline--tRNA ligase (A1KUG4)
Analyse AlphaFold monomer V2.0 prediction for proline--tRNA ligase (A1KUG4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1KUG4
- Type
- protein
- Length
- 570 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9073C46348542FfE4327c3F363F9B51B22058e75
- Molecule
- Proline--tRNA ligase
- UniProt
- A1KUG4
- Pockets
- 4 · best druggability 0.70
Structure
1 distinct chain · 29% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline--tRNA ligase | protein | 570 | 29% helix, 30% strand | A1KUG4 |
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 | 454 | 0.70 | 0.81 | 50 | empty |
| 2 | 110 | 0.45 | 0.78 | 23 | empty |
| 3 | 85 | 0.36 | 0.76 | 16 | empty |
| 4 | 57 | 0.33 | 0.77 | 16 | 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 A1KUG4
- Elsewhere: UniProt A1KUG4 · AlphaFold DB A1KUG4
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