Research workbench
AlphaFold monomer V2.0 prediction for pyrroline-5-carboxylate reductase (P0A9L8)
Analyse AlphaFold monomer V2.0 prediction for pyrroline-5-carboxylate reductase (P0A9L8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0A9L8
- Type
- protein
- Length
- 269 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0002Ae91B0FDC26aE76c036F024CE258FeB6d459
- Molecule
- Pyrroline-5-carboxylate reductase
- UniProt
- P0A9L8
- Pockets
- 3 · best druggability 0.59
Structure
1 distinct chain · 60% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyrroline-5-carboxylate reductase | protein | 269 | 60% helix, 13% strand | P0A9L8 |
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 | 492 | 0.59 | 0.73 | 46 | empty |
| 2 | 77 | 0.33 | 0.74 | 17 | empty |
| 3 | 52 | 0.27 | 0.74 | 18 | 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 P0A9L8
- Elsewhere: UniProt P0A9L8 · AlphaFold DB P0A9L8
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