Research workbench
AlphaFold monomer V2.0 prediction for vacuolar membrane protease (C5DDZ2)
Analyse AlphaFold monomer V2.0 prediction for vacuolar membrane protease (C5DDZ2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5DDZ2
- Type
- protein
- Length
- 962 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC568E62d5F08a237227D0b8bd20415100A62a6e2
- Molecule
- Vacuolar membrane protease
- UniProt
- C5DDZ2
- Pockets
- 8 · best druggability 0.81
Structure
1 distinct chain · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar membrane protease | protein | 962 | 41% helix, 19% strand | C5DDZ2 |
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 | 1020 | 0.81 | 0.82 | 97 | empty |
| 2 | 473 | 0.69 | 0.80 | 61 | empty |
| 3 | 564 | 0.66 | 0.77 | 45 | empty |
| 4 | 113 | 0.41 | 0.76 | 17 | empty |
| 5 | 75 | 0.38 | 0.78 | 21 | 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 C5DDZ2
- Elsewhere: UniProt C5DDZ2 · AlphaFold DB C5DDZ2
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