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AlphaFold monomer V2.0 prediction for vacuolar fusion protein MON1 homolog B (Q7L1V2)
Analyse AlphaFold monomer V2.0 prediction for vacuolar fusion protein MON1 homolog B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7L1V2
- Type
- protein
- Length
- 547 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf99Dfb88a9dDC28BfCf98bd01481300A29a317a9
- Molecule
- Vacuolar fusion protein MON1 homolog B
- UniProt
- Q7L1V2
- Pockets
- 4 · best druggability 0.68
Structure
1 distinct chain · 33% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar fusion protein MON1 homolog B | protein | 547 | 33% helix, 20% strand | Q7L1V2 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.68 | 0.93 | 22 | empty |
| 2 | 397 | 0.68 | 0.81 | 63 | empty |
| 3 | 409 | 0.59 | 0.75 | 40 | empty |
| 4 | 59 | 0.32 | 0.77 | 17 | 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 Q7L1V2
- Elsewhere: UniProt Q7L1V2 · AlphaFold DB Q7L1V2
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