Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase proenzyme (A7NAF0)
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
- A7NAF0
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- Phosphatidylserine decarboxylase proenzyme
- UniProt
- A7NAF0
- Pockets
- 5 · best druggability 0.42
Structure
1 distinct chain · 23% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylserine decarboxylase proenzyme | protein | 283 | 23% helix, 35% strand | A7NAF0 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.42 | 0.81 | 16 | empty |
| 2 | 83 | 0.40 | 0.78 | 16 | empty |
| 3 | 69 | 0.39 | 0.79 | 16 | empty |
| 4 | 73 | 0.35 | 0.76 | 16 | empty |
| 5 | 66 | 0.35 | 0.76 | 11 | 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 A7NAF0
- Elsewhere: UniProt A7NAF0 · AlphaFold DB A7NAF0
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