Fig. 3From: Prevalence of CYP17A1 gene mutations in 17α-hydroxylase deficiency in the Chinese Han populationFerroheme binding region before and after amino acid changes. a Normal ferroheme binding region in the protein active center. Arg440 and heme formed 2 hydrogen bonds in the protein active center, and Pro434 and Phe453 were essential in stabilizing the β-fold and J-helix structure around the active center. b Ferroheme binding region in the protein active center after mutation. The Tyr329Lys mutation caused a shortened protein missing the amino acids after 417, which directly damaged the functional region after the ferroheme binding region shifted after losing the hydrogen bond and the upper left shift of preserved Arg409, Ser411 and Val416Back to article page