Research workbench
AlphaFold monomer V2.0 prediction for vacuolar membrane protease (A7TM20)
Analyse AlphaFold monomer V2.0 prediction for vacuolar membrane protease (A7TM20) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7TM20
- Type
- protein
- Length
- 939 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
- Molecule
- Vacuolar membrane protease
- UniProt
- A7TM20
- Pockets
- 8 · best druggability 0.77
Structure
1 distinct chain · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar membrane protease | protein | 939 | 44% helix, 19% strand | A7TM20 |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 953 | 0.77 | 0.79 | 77 | empty |
| 2 | 376 | 0.67 | 0.80 | 50 | empty |
| 3 | 186 | 0.63 | 0.83 | 24 | empty |
| 4 | 273 | 0.57 | 0.77 | 27 | empty |
| 5 | 156 | 0.44 | 0.74 | 20 | 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 A7TM20
- Elsewhere: UniProt A7TM20 · AlphaFold DB A7TM20
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