Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase proenzyme (B6J316)
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
- B6J316
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x66026B7eDA2C7707c7042FCF1BE7d1A483c4dD3c
- Molecule
- Phosphatidylserine decarboxylase proenzyme
- UniProt
- B6J316
- Pockets
- 6 · best druggability 0.49
Structure
1 distinct chain · 23% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylserine decarboxylase proenzyme | protein | 282 | 23% helix, 34% strand | B6J316 |
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 166 | 0.49 | 0.77 | 29 | empty |
| 2 | 67 | 0.40 | 0.80 | 21 | empty |
| 3 | 57 | 0.37 | 0.79 | 15 | empty |
| 4 | 56 | 0.34 | 0.78 | 12 | empty |
| 5 | 53 | 0.34 | 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 B6J316
- Elsewhere: UniProt B6J316 · AlphaFold DB B6J316
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