Research workbench
AlphaFold monomer V2.0 prediction for vacuolar membrane protease (C4R628)
Analyse AlphaFold monomer V2.0 prediction for vacuolar membrane protease (C4R628) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C4R628
- Type
- protein
- Length
- 990 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Vacuolar membrane protease
- UniProt
- C4R628
- Pockets
- 13 · best druggability 0.79
Structure
1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar membrane protease | protein | 990 | 40% helix, 19% strand | C4R628 |
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 769 | 0.79 | 0.82 | 71 | empty |
| 2 | 457 | 0.67 | 0.78 | 50 | empty |
| 3 | 212 | 0.66 | 0.83 | 25 | empty |
| 4 | 203 | 0.62 | 0.82 | 28 | empty |
| 5 | 301 | 0.60 | 0.78 | 35 | 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 C4R628
- Elsewhere: UniProt C4R628 · AlphaFold DB C4R628
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