Research workbench
AlphaFold monomer V2.0 prediction for vacuolar import and degradation protein 22 (Q05934)
Analyse AlphaFold monomer V2.0 prediction for vacuolar import and degradation protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q05934
- Type
- protein
- Length
- 901 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- Vacuolar import and degradation protein 22
- UniProt
- Q05934
- Pockets
- 11 · best druggability 0.64
Structure
1 distinct chain · 47% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar import and degradation protein 22 | protein | 901 | 47% helix, 10% strand | Q05934 |
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 498 | 0.64 | 0.76 | 39 | empty |
| 2 | 514 | 0.63 | 0.75 | 57 | empty |
| 3 | 130 | 0.55 | 0.82 | 21 | empty |
| 4 | 285 | 0.51 | 0.74 | 40 | empty |
| 5 | 62 | 0.47 | 0.84 | 15 | empty |
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 Q05934
- Elsewhere: UniProt Q05934 · AlphaFold DB Q05934
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