Research workbench
AlphaFold monomer V2.0 prediction for vacuolar membrane protease (A4R254)
Analyse AlphaFold monomer V2.0 prediction for vacuolar membrane protease (A4R254) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4R254
- Type
- protein
- Length
- 1,011 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- Vacuolar membrane protease
- UniProt
- A4R254
- Pockets
- 11 · best druggability 0.80
Structure
1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar membrane protease | protein | 1011 | 40% helix, 17% strand | A4R254 |
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1033 | 0.80 | 0.81 | 98 | empty |
| 2 | 272 | 0.62 | 0.80 | 26 | empty |
| 3 | 176 | 0.53 | 0.80 | 32 | empty |
| 4 | 114 | 0.49 | 0.80 | 22 | empty |
| 5 | 88 | 0.48 | 0.82 | 20 | empty |
Modifications
Observed in the structure: 1 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 A4R254
- Elsewhere: UniProt A4R254 · AlphaFold DB A4R254
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