Research workbench
AlphaFold monomer V2.0 prediction for proline--tRNA ligase (A1APU5)
Analyse AlphaFold monomer V2.0 prediction for proline--tRNA ligase (A1APU5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1APU5
- Type
- protein
- Length
- 576 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Proline--tRNA ligase
- UniProt
- A1APU5
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 31% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline--tRNA ligase | protein | 576 | 31% helix, 30% strand | A1APU5 |
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 | 571 | 0.71 | 0.79 | 55 | empty |
| 2 | 81 | 0.50 | 0.83 | 23 | empty |
| 3 | 75 | 0.33 | 0.76 | 19 | empty |
| 4 | 55 | 0.31 | 0.76 | 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 A1APU5
- Elsewhere: UniProt A1APU5 · AlphaFold DB A1APU5
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