Research workbench
AlphaFold monomer V2.0 prediction for thioredoxin domain-containing protein 3 homolog (P90666)
Analyse AlphaFold monomer V2.0 prediction for thioredoxin domain-containing protein 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P90666
- Type
- protein
- Length
- 837 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2a7AdD564c0554f2678aF0B7b36468EdBbF1e6D5
- Molecule
- Thioredoxin domain-containing protein 3 homolog
- UniProt
- P90666
- Pockets
- 5 · best druggability 0.62
Structure
1 distinct chain · 34% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin domain-containing protein 3 homolog | protein | 837 | 34% helix, 14% strand | P90666 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 293 | 0.62 | 0.80 | 42 | empty |
| 2 | 147 | 0.55 | 0.82 | 25 | empty |
| 3 | 199 | 0.50 | 0.77 | 32 | empty |
| 4 | 73 | 0.34 | 0.75 | 14 | empty |
| 5 | 61 | 0.29 | 0.74 | 14 | 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 P90666
- Elsewhere: UniProt P90666 · AlphaFold DB P90666
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