Research workbench
AlphaFold monomer V2.0 prediction for pyrroline-5-carboxylate reductase 1 (E0TY11)
Analyse AlphaFold monomer V2.0 prediction for pyrroline-5-carboxylate reductase 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- E0TY11
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Pyrroline-5-carboxylate reductase 1
- UniProt
- E0TY11
- Pockets
- 4 · best druggability 0.47
Structure
1 distinct chain · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyrroline-5-carboxylate reductase 1 | protein | 297 | 56% helix, 12% strand | E0TY11 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 137 | 0.47 | 0.78 | 26 | empty |
| 2 | 152 | 0.46 | 0.76 | 21 | empty |
| 3 | 150 | 0.40 | 0.73 | 22 | empty |
| 4 | 92 | 0.33 | 0.72 | 19 | 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 E0TY11
- Elsewhere: UniProt E0TY11 · AlphaFold DB E0TY11
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