Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase proenzyme (B0B8S5)
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
- B0B8S5
- Type
- protein
- Length
- 301 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7A237143798c68038d48886A489bD0505943F92E
- Molecule
- Phosphatidylserine decarboxylase proenzyme
- UniProt
- B0B8S5
- Pockets
- 3 · best druggability 0.66
Structure
1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylserine decarboxylase proenzyme | protein | 301 | 30% helix, 27% strand | B0B8S5 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 350 | 0.66 | 0.80 | 34 | empty |
| 2 | 247 | 0.64 | 0.82 | 26 | empty |
| 3 | 212 | 0.51 | 0.76 | 18 | 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 B0B8S5
- Elsewhere: UniProt B0B8S5 · AlphaFold DB B0B8S5
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