Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase proenzyme (Q7MYS6)
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
- Q7MYS6
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x278079ff53c25d5184a04C97Cc641066644dc05e
- Molecule
- Phosphatidylserine decarboxylase proenzyme
- UniProt
- Q7MYS6
- Pockets
- 3 · best druggability 0.40
Structure
1 distinct chain · 22% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylserine decarboxylase proenzyme | protein | 297 | 22% helix, 33% strand | Q7MYS6 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.40 | 0.79 | 18 | empty |
| 2 | 91 | 0.39 | 0.76 | 20 | empty |
| 3 | 53 | 0.28 | 0.75 | 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 Q7MYS6
- Elsewhere: UniProt Q7MYS6 · AlphaFold DB Q7MYS6
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