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Literature summary for 5.3.4.1 extracted from
- Protein disulfide isomerase, a multifunctional protein chaperone, shows copper-binding activity (2003), Biochem. Biophys. Res. Commun., 311, 405-414.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression Escherichia coli | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum | - |
Homo sapiens | 5783 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ag+ | PDI binds Ag+ | Homo sapiens |  |
| Ca2+ | major calcium binding protein of the endoplasmic reticulum | Homo sapiens | |
| Cu2+ | PDI binds a maximum of 4 mol Cu2+ and is able to reduce it to Cu+, the bound Cu+ is surface-exposed | Homo sapiens | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant PDI | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| unfolded RNase A | - |
Homo sapiens | refolded RNase A | - |
? | |
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Release 2023.1 (January 2023)
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