Research workbench
AlphaFold monomer V2.0 prediction for vacuolar membrane protease (E9E6S9)
Analyse AlphaFold monomer V2.0 prediction for vacuolar membrane protease (E9E6S9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- E9E6S9
- Type
- protein
- Length
- 1,029 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC631cbCDF0F9A68578F6bb83aD28877742912F30
- Molecule
- Vacuolar membrane protease
- UniProt
- E9E6S9
- Pockets
- 10 · best druggability 0.78
Structure
1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar membrane protease | protein | 1029 | 38% helix, 17% strand | E9E6S9 |
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1073 | 0.78 | 0.80 | 87 | empty |
| 2 | 300 | 0.67 | 0.81 | 26 | empty |
| 3 | 102 | 0.60 | 0.87 | 21 | empty |
| 4 | 297 | 0.55 | 0.76 | 34 | empty |
| 5 | 162 | 0.52 | 0.80 | 32 | 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 E9E6S9
- Elsewhere: UniProt E9E6S9 · AlphaFold DB E9E6S9
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