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.
The study of hephaestin's structure is based on comparing it to ceruloplasmin's structure, which has been determined through crystallography. This comparison reveals that many structural features important for the enzymatic activity of both proteins are conserved. These shared features include cysteine residues involved in disulfide bond formation, histidine residues involved in copper binding, and residues responsible for iron substrate binding.