Research workbench
AlphaFold monomer V2.0 prediction for thiosulfate dehydrogenase electron acceptor (D5WYQ6)
Analyse AlphaFold monomer V2.0 prediction for thiosulfate dehydrogenase electron… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- D5WYQ6
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- Molecule
- Thiosulfate dehydrogenase electron acceptor
- UniProt
- D5WYQ6
- Pockets
- 3 · best druggability 0.78
Structure
1 distinct chain · 47% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thiosulfate dehydrogenase electron acceptor | protein | 217 | 47% helix, 4% strand | D5WYQ6 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.78 | 0.92 | 38 | empty |
| 2 | 203 | 0.65 | 0.83 | 34 | empty |
| 3 | 53 | 0.32 | 0.77 | 16 | 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 D5WYQ6
- Elsewhere: UniProt D5WYQ6 · AlphaFold DB D5WYQ6
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