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Literature summary for 4.6.1.23 extracted from
- Binding and enzymatic properties of ageritin, a fungal ribotoxin with novel zinc-dependent function (2019), Int. J. Biol. Macromol., 136, 625-631 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| modeling of the catalytic metal binding site of ageritin, made of the putative triad Asp68, Asp70 and His77. Ageritin has the structure and function of an RNase but a Mg2+/Zn2+-dependent mechanism of action | Cyclocybe aegerita |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | - |
Cyclocybe aegerita |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | ageritin's ribonucleolytic activity requires the presence of divalent cations, with a maximum activation in the presence of zinc ions | Cyclocybe aegerita | |
| Zinc | maximum activation in the presence of zinc ions | Cyclocybe aegerita | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cyclocybe aegerita | C0HLG3 | - |
- |
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Release 2023.1 (January 2023)
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