Research workbench
AlphaFold monomer V2.0 prediction for high osmolarity signaling protein SHO1 (B2VV00)
Analyse AlphaFold monomer V2.0 prediction for high osmolarity signaling protein SHO1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2VV00
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- High osmolarity signaling protein SHO1
- UniProt
- B2VV00
- Pockets
- 2 · best druggability 0.43
Structure
1 distinct chain · 39% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High osmolarity signaling protein SHO1 | protein | 295 | 39% helix, 8% strand | B2VV00 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.43 | 0.80 | 15 | empty |
| 2 | 58 | 0.43 | 0.83 | 13 | 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 B2VV00
- Elsewhere: UniProt B2VV00 · AlphaFold DB B2VV00
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