Protein Domain : 2Fe-2S ferredoxin-type iron-sulfur binding domain IPR001041

Type	Domain
Description	Ferredoxins are small, acidic, electron transfer proteins that are ubiquitous in biological redox systems. They have either 4Fe-4S, 3Fe-4S, or 2Fe-2Scluster. Among them, ferredoxin with one 2Fe-2S cluster per molecule are present in plants, animals, and bacteria, and form a distinct Ferredoxinfamily [ ]. 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.Several structures of the 2Fe-2S ferredoxin-type domain have been determined [ ]. The domain is classified as a β-grasp, which is characterised as having a β-sheet comprised of four β-strands and one α-helix flanking the sheet. The two Fe atoms are coordinated tetrahedrally by the two inorganic S atoms and four cysteinyl S atoms.
Short Name	2Fe-2S_ferredoxin-type