Research workbench
AlphaFold monomer V2.0 prediction for pyrrolidone-carboxylate peptidase (Q5JEL5)
Analyse AlphaFold monomer V2.0 prediction for pyrrolidone-carboxylate peptidase (Q5JEL5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5JEL5
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xfB234317515f73C4d96eAfC2eBb80D4fa77E633a
- Molecule
- Pyrrolidone-carboxylate peptidase
- UniProt
- Q5JEL5
- Pockets
- 1 · best druggability 0.46
Structure
1 distinct chain · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyrrolidone-carboxylate peptidase | protein | 206 | 34% helix, 25% strand | Q5JEL5 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.46 | 0.77 | 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 Q5JEL5
- Elsewhere: UniProt Q5JEL5 · AlphaFold DB Q5JEL5
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