Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase proenzyme (A7MZ50)
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
- A7MZ50
- Type
- protein
- Length
- 285 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5b13c9115B53001a236cd5DD3D2992124e9b8fF1
- Molecule
- Phosphatidylserine decarboxylase proenzyme
- UniProt
- A7MZ50
- Pockets
- 3 · best druggability 0.48
Structure
1 distinct chain · 22% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylserine decarboxylase proenzyme | protein | 285 | 22% helix, 35% strand | A7MZ50 |
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 | 179 | 0.48 | 0.76 | 31 | empty |
| 2 | 68 | 0.37 | 0.78 | 16 | empty |
| 3 | 61 | 0.30 | 0.75 | 15 | 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 A7MZ50
- Elsewhere: UniProt A7MZ50 · AlphaFold DB A7MZ50
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