Research workbench
AlphaFold monomer V2.0 prediction for vacuolar membrane protease (C5P998)
Analyse AlphaFold monomer V2.0 prediction for vacuolar membrane protease (C5P998) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5P998
- Type
- protein
- Length
- 1,012 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
- Molecule
- Vacuolar membrane protease
- UniProt
- C5P998
- Pockets
- 12 · best druggability 0.78
Structure
1 distinct chain · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar membrane protease | protein | 1012 | 37% helix, 17% strand | C5P998 |
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1177 | 0.78 | 0.80 | 94 | empty |
| 2 | 258 | 0.61 | 0.79 | 27 | empty |
| 3 | 199 | 0.55 | 0.79 | 29 | empty |
| 4 | 100 | 0.54 | 0.84 | 18 | empty |
| 5 | 136 | 0.49 | 0.79 | 31 | 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 C5P998
- Elsewhere: UniProt C5P998 · AlphaFold DB C5P998
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