Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase proenzyme (B7V346)
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
- B7V346
- Type
- protein
- Length
- 289 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe98bf0c02d2A46E3299A9930210B6C72162719bF
- Molecule
- Phosphatidylserine decarboxylase proenzyme
- UniProt
- B7V346
- Pockets
- 4 · best druggability 0.48
Structure
1 distinct chain · 24% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylserine decarboxylase proenzyme | protein | 289 | 24% helix, 33% strand | B7V346 |
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 | 142 | 0.48 | 0.77 | 28 | empty |
| 2 | 66 | 0.42 | 0.81 | 21 | empty |
| 3 | 64 | 0.37 | 0.78 | 16 | empty |
| 4 | 73 | 0.37 | 0.78 | 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 B7V346
- Elsewhere: UniProt B7V346 · AlphaFold DB B7V346
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