MolNFT v1 · #290142 · protein
AlphaFold monomer V2.0 prediction for pyrrolidone-carboxylate peptidase (O58321)
O58321: “AlphaFold monomer V2.0 prediction for pyrrolidone-carboxylate peptidase (O58321)”. 1 pocket (best druggability 0.48). MolNFT v1 #290142 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- O58321
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa4c1cb262579E9bA578f7bEf2fca986dddAA715E
- Molecule
- Pyrrolidone-carboxylate peptidase
- UniProt
- O58321
- Pockets
- 1 · best druggability 0.48
Structure
1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyrrolidone-carboxylate peptidase | protein | 206 | 39% helix, 21% strand | O58321 |
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 | 100 | 0.48 | 0.81 | 22 | empty |
Compared structures
- 1IU8 · The X-ray Crystal Structure of Pyrrolidone-Carboxylate Peptidase from Hyperthermophilic… · an experimental structure of the same protein · chain A against A, TM-score 1.00
- 1IU8 · The X-ray crystal structure of pyrrolidone-carboxylate peptidase from hyperthermophilic… · an experimental structure of the same protein · chain A against A, TM-score 1.00
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 O58321
- Elsewhere: UniProt O58321 · AlphaFold DB O58321
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