Comparative models of hephaestin's structure have been created using established crystallographic data from ceruloplasmin, and these studies suggest that many of the structural features important in the enzymatic function of the latter are also conserved in the former. In particular, these shared features include cysteine residues involved in disulfide bond formation, histidine residues involved in copper binding, and residues involved in the binding of the iron substrate.
Comparative studies of hephaestin and ceruloplasmin have revealed that many structural features crucial for their respective enzymatic functions are conserved between the two proteins. These shared features include cysteine residues involved in disulfide bond formation, histidine residues involved in copper binding, and residues responsible for iron substrate binding.