Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
copper | the acetyl-CoA synthase active site contains a [4Fe-4S] cluster bridged to a binuclear Cu-Ni site. Distorted Cu(I)-S3 site in the fully active enzyme in solution. Average Cu-S bond length of 2.25 A and a metal neighbor at 2.65 A, consistent with the Cu-Ni distance observed in the crystal structure. Cu-SCoA intermediate in the mechanism of acetyl-CoA synthesis. Essential and functional role for copper in the enzyme | Moorella thermoacetica | |
Iron | the acetyl-CoA synthase active site contains a [4Fe-4S] cluster bridged to a binuclear Cu-Ni site | Moorella thermoacetica | |
Nickel | the acetyl-CoA synthase active site contains a [4Fe-4S] cluster bridged to a binuclear Cu-Ni site. Distorted Cu(I)-S3 site in the fully active enzyme in solution. Average Cu-S bond length of 2.25 A and a metal neighbor at 2.65 A, consistent with the Cu-Ni distance observed in the crystal structure | Moorella thermoacetica |
Organism | UniProt | Comment | Textmining |
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Moorella thermoacetica | - |
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