Research workbench
AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein VTA1 homolog (Q9CR26)
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
- Q9CR26
- Type
- protein
- Length
- 309 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1C9610A440a2df878b14E60F32F675a1820EEd0a
- Molecule
- Vacuolar protein sorting-associated protein VTA1 homolog
- UniProt
- Q9CR26
- Pockets
- 4 · best druggability 0.59
Structure
1 distinct chain · 53% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar protein sorting-associated protein VTA1 homolog | protein | 309 | 53% helix, 0% strand | Q9CR26 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.59 | 0.83 | 24 | empty |
| 2 | 110 | 0.47 | 0.80 | 19 | empty |
| 3 | 51 | 0.32 | 0.77 | 13 | empty |
| 4 | 61 | 0.27 | 0.73 | 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 Q9CR26
- Elsewhere: UniProt Q9CR26 · AlphaFold DB Q9CR26
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