Research workbench
AlphaFold monomer V2.0 prediction for vacuolar membrane protease (B0XPG0)
Analyse AlphaFold monomer V2.0 prediction for vacuolar membrane protease (B0XPG0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B0XPG0
- Type
- protein
- Length
- 965 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- Vacuolar membrane protease
- UniProt
- B0XPG0
- Pockets
- 8 · best druggability 0.79
Structure
1 distinct chain · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar membrane protease | protein | 965 | 38% helix, 18% strand | B0XPG0 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1017 | 0.79 | 0.80 | 95 | empty |
| 2 | 325 | 0.67 | 0.81 | 29 | empty |
| 3 | 94 | 0.63 | 0.89 | 17 | empty |
| 4 | 129 | 0.38 | 0.74 | 24 | empty |
| 5 | 88 | 0.38 | 0.77 | 22 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 B0XPG0
- Elsewhere: UniProt B0XPG0 · AlphaFold DB B0XPG0
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