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Literature summary extracted from
- A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units (1998), Nat. Struct. Biol., 5, 602-611.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.8.99.B1 | expression in Escherichia coli | Pyrococcus furiosus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.8.99.B1 | - |
Pyrococcus furiosus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.99.B1 | Pyrococcus furiosus | Q51760 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.8.99.B1 | - |
Pyrococcus furiosus |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.8.99.B1 | dimer | the protein consists of two homologous structural units with low sequence identity. Each unit contains a thioredoxin fold with a distinct CXXC active site motif | Pyrococcus furiosus |
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Release 2023.1 (January 2023)
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