Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase proenzyme (Q1LSP9)
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
- Q1LSP9
- Type
- protein
- Length
- 292 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC247c99E05131ed14368eDD5e659B4F41aFA32ab
- Molecule
- Phosphatidylserine decarboxylase proenzyme
- UniProt
- Q1LSP9
- Pockets
- 4 · best druggability 0.70
Structure
1 distinct chain · 23% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylserine decarboxylase proenzyme | protein | 292 | 23% helix, 33% strand | Q1LSP9 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 131 | 0.70 | 0.90 | 24 | empty |
| 2 | 94 | 0.43 | 0.79 | 16 | empty |
| 3 | 95 | 0.34 | 0.73 | 14 | empty |
| 4 | 51 | 0.30 | 0.76 | 12 | 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 Q1LSP9
- Elsewhere: UniProt Q1LSP9 · AlphaFold DB Q1LSP9
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