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Ferrochelatase
From Proteopedia
Ferrochelatase (FECH) catalyzes the last step in the formation of heme. FECH adds Fe+2 to protoporphyrin IX converting it to protoheme. The human FECH is a homodimer containing 2 similar domains and an iron-sulfur cluster. Defective FECH is the cause of porphyria.
3D structures of ferrochelatase
1ak1 – BsFECH – Bacillus subtilis
2ac4 - BsFECH (mutant)
1doz - BsFECH + Mg
1ld3 - BsFECH + Zn
2ac2 - BsFECH (mutant) + Zn
2h1v, 3goq - BsFECH (mutant) + Mg
2h1w - BsFECH (mutant) + Fe + Mg
2hk6 - BsFECH + Fe+ Mg
1n0i - BsFECH + Cd + Mg
3m4z - BsFECH + Co + Mg
1l8x - yFECH + Co – yeast
1lbq - yFECH
2qd4 - hFECH + Fe2S2 - human
1hrk, 2pnj, 2po5, 2po7, 3aqi, 4f4d - hFECH (mutant) + Fe2S2
Ferrochelatase complex with porphyrin
2qd3, 3hcn, 3hco, 3hcp - hFECH + protoporphyrin IX + Fe2S2
3hcr - hFECH + protoporphyrin IX + O2 + Fe2S2
2hre, 2qd1, 2qd2 - hFECH (mutant) + protoporphyrin IX + Fe2S2
2qd5 - hFECH + protoporphyrin IX + Pb + Fe2S2
1c1h - BsFECH + N-methylmesoporphyrin + Mg
2q3j, 2q2o - BsFECH (mutant) + N-methylmesoporphyrin + Mg
2q2n – BsFECH + protoporphyrin IX + Mg
1c9e]] - BsFECH + N-methylmesoporphyrin + Cu + Mg
