Research workbench
AlphaFold monomer V2.0 prediction for cortical fragment-lytic enzyme (P0DPJ9)
Analyse AlphaFold monomer V2.0 prediction for cortical fragment-lytic enzyme (P0DPJ9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0DPJ9
- Type
- protein
- Length
- 430 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xaa53776A41fB2e67da75A96E8a53746b6874aAB4
- Molecule
- Cortical fragment-lytic enzyme
- UniProt
- P0DPJ9
- Pockets
- 4 · best druggability 0.62
Structure
1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cortical fragment-lytic enzyme | protein | 430 | 36% helix, 23% strand | P0DPJ9 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.62 | 0.85 | 35 | empty |
| 2 | 329 | 0.57 | 0.75 | 35 | empty |
| 3 | 71 | 0.33 | 0.75 | 15 | empty |
| 4 | 50 | 0.31 | 0.77 | 14 | 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 P0DPJ9
- Elsewhere: UniProt P0DPJ9 · AlphaFold DB P0DPJ9
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