Fe2S2 Ferredoxins
| 2Fe-2S iron-sulfur cluster binding domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Structural representation of an Fe2S2 ferredoxin. | |||||||||
| Identifiers | |||||||||
| Symbol | Fer2 | ||||||||
| Pfam | PF00111 | ||||||||
| InterPro | IPR001041 | ||||||||
| PROSITE | PDOC00642 | ||||||||
| SCOP | 3fxc | ||||||||
| SUPERFAMILY | 3fxc | ||||||||
| OPM protein | 1kf6 | ||||||||
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Members of the 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2), which includes putidaredoxin and terpredoxin, and adrenodoxin. They are proteins of around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This conserved region is also found as a domain in various metabolic enzymes and in multidomain proteins, such as aldehyde oxidoreductase (N-terminal), xanthine oxidase (N-terminal), phthalate dioxygenase reductase (C-terminal), succinate dehydrogenase iron-sulphur protein (N-terminal), and methane monooxygenase reductase (N-terminal).
Read more about this topic: Ferredoxin