Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase proenzyme (Q1I433)
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
- Q1I433
- Type
- protein
- Length
- 287 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2C851c3fFC4b4Dc5b51504CB30d0Af69138d2CCC
- Molecule
- Phosphatidylserine decarboxylase proenzyme
- UniProt
- Q1I433
- Pockets
- 4 · best druggability 0.48
Structure
1 distinct chain · 23% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylserine decarboxylase proenzyme | protein | 287 | 23% helix, 33% strand | Q1I433 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 131 | 0.48 | 0.78 | 24 | empty |
| 2 | 63 | 0.40 | 0.81 | 21 | empty |
| 3 | 62 | 0.36 | 0.78 | 14 | empty |
| 4 | 52 | 0.32 | 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 Q1I433
- Elsewhere: UniProt Q1I433 · AlphaFold DB Q1I433
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