Research workbench
AlphaFold monomer V2.0 prediction for thioredoxin reductase (P9WHH1)
Analyse AlphaFold monomer V2.0 prediction for thioredoxin reductase (P9WHH1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P9WHH1
- Type
- protein
- Length
- 335 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x59018c174d1Ecad02850b8c56eDC5A53F1C2d4c5
- Molecule
- Thioredoxin reductase
- UniProt
- P9WHH1
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 26% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin reductase | protein | 335 | 26% helix, 26% strand | P9WHH1 |
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 | 535 | 0.76 | 0.83 | 68 | empty |
| 2 | 231 | 0.51 | 0.76 | 31 | empty |
| 3 | 52 | 0.25 | 0.73 | 20 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P9WHH1
- Elsewhere: UniProt P9WHH1 · AlphaFold DB P9WHH1
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