Research workbench
AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein 72 homolog (Q9VKM6)
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
- Q9VKM6
- Type
- protein
- Length
- 351 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x97EfFf2d74994e28D3b69b1503Bd9c292B2Df480
- Molecule
- Vacuolar protein sorting-associated protein 72 homolog
- UniProt
- Q9VKM6
- Pockets
- 1 · best druggability 0.28
Structure
1 distinct chain · 37% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar protein sorting-associated protein 72 homolog | protein | 351 | 37% helix, 8% strand | Q9VKM6 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.28 | 0.74 | 11 | empty |
Compared structures
- 5CHL · Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1… · an experimental structure of the same protein · chain A against A, TM-score 0.14
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 Q9VKM6
- Elsewhere: UniProt Q9VKM6 · AlphaFold DB Q9VKM6
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