Multiple structure-based sequence alignment of FeADHs with a known 3D structure (residues 1–250 according to human ADHFE1).

<p>These proteins belong to five different subfamilies of the FeADH family. For comparison, ADHFE1 sequence from human is included in the alignment, as well as four glycerol dehydrogenase sequences with a known three-dimensional structure. PDB accession number of each sequence is indicated at the left side of alignment, whereas the protein subfamily to which each sequence belongs, is in the right side of the alignment. Conserved β-strands and α-helices for each structure are indicated in yellow and green, respectively. Residue position determinant for coenzyme specificity is indicated with a red square. Residues involved in the binding of Fe atom are highlighted in pink; residues involved in the binding of Zinc atom in glicerol dehydrogenases are highlighted in grey. Amino acid residues from human ADHFE1 sequence, highlighted in blue and grey indicate positions that belong to the N-terminal or C-terminal domains, respectively. The three-dimensional alignment of FeADH structures was performed using the VAST tool at the NCBI’s server [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0166851#pone.0166851.ref043" target="_blank">43</a>].