Research workbench
AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein 41 homolog (Q19954)
Analyse AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q19954
- Type
- protein
- Length
- 901 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- Molecule
- Vacuolar protein sorting-associated protein 41 homolog
- UniProt
- Q19954
- Pockets
- 4 · best druggability 0.79
Structure
1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar protein sorting-associated protein 41 homolog | protein | 901 | 42% helix, 21% strand | Q19954 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 763 | 0.79 | 0.82 | 58 | empty |
| 2 | 50 | 0.53 | 0.88 | 17 | empty |
| 3 | 72 | 0.48 | 0.83 | 14 | empty |
| 4 | 68 | 0.33 | 0.75 | 10 | 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 Q19954
- Elsewhere: UniProt Q19954 · AlphaFold DB Q19954
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