Research workbench
AlphaFold monomer V2.0 prediction for high osmolarity signaling protein SHO1 (E5AD87)
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
- E5AD87
- Type
- protein
- Length
- 336 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- High osmolarity signaling protein SHO1
- UniProt
- E5AD87
- Pockets
- 1 · best druggability 0.72
Structure
1 distinct chain · 37% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High osmolarity signaling protein SHO1 | protein | 336 | 37% helix, 7% strand | E5AD87 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 587 | 0.72 | 0.80 | 52 | 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 E5AD87
- Elsewhere: UniProt E5AD87 · AlphaFold DB E5AD87
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