Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase proenzyme (Q24UV7)
Analyse AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q24UV7
- Type
- protein
- Length
- 298 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xAaA863E14cD17cb4c26e239Ad348e822228468a2
- Molecule
- Phosphatidylserine decarboxylase proenzyme
- UniProt
- Q24UV7
- Pockets
- 4 · best druggability 0.65
Structure
1 distinct chain · 27% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylserine decarboxylase proenzyme | protein | 298 | 27% helix, 30% strand | Q24UV7 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 196 | 0.65 | 0.84 | 35 | empty |
| 2 | 162 | 0.52 | 0.78 | 22 | empty |
| 3 | 203 | 0.51 | 0.77 | 25 | empty |
| 4 | 50 | 0.33 | 0.78 | 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 Q24UV7
- Elsewhere: UniProt Q24UV7 · AlphaFold DB Q24UV7
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