Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase proenzyme (Q0VMD7)
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
- Q0VMD7
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x638EA7d798aBF8bbDfE1dCA65BB71AD6E3a92db9
- Molecule
- Phosphatidylserine decarboxylase proenzyme
- UniProt
- Q0VMD7
- Pockets
- 4 · best druggability 0.53
Structure
1 distinct chain · 23% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylserine decarboxylase proenzyme | protein | 291 | 23% helix, 32% strand | Q0VMD7 |
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 | 169 | 0.53 | 0.79 | 30 | empty |
| 2 | 77 | 0.44 | 0.81 | 20 | empty |
| 3 | 91 | 0.39 | 0.77 | 19 | empty |
| 4 | 71 | 0.33 | 0.76 | 20 | 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 Q0VMD7
- Elsewhere: UniProt Q0VMD7 · AlphaFold DB Q0VMD7
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