The final model of CsTegu20.6 consisted of two domains: a N-terminal domain (calcium-binding domain) and a C-terminal domain (DLC domain) adopting a classic ferredoxin fold , which forms a four-stranded antiparallel β-sheet flanked on one side by two α-helices (Figure 5A,B). However, unlike a typical ferredoxin fold associated with the overall symmetry of β-α-β-β-α-β, the β1-α5-α6-β2-β3-β4 fold was present in the DLC domain of CsTegu20.6. The two α-helices, α6 and α7, were packed in an antiparallel hairpin structure against the β-sheet with four antiparallel β-strands, β1-β3-β4-β2. These findings are in line with structural data obtained from a DALI search  that found similarities to numerous proteins with DLC1 (also known as DLC8), such as 5E0M and 3DVT, the structures of which represent the same fold . DLC-containing proteins can form homodimers through hydrogen bonds, backbone-side chain electrostatic interactions and van der Waals contacts between side chains . Previous studies have indicated that the homodimeric DLCs in S. mansoni  and F. hepatica  were composed of two asymmetric monomers through β-sheet interactions. The homodimer of CsTegu20.6 was constructed using GalaxyGemini  with only the C chain of DLC1 (PDB ID: 4DS1_C), although the fifth β-strand (indicated with a dotted circles) as a monomeric counterpart was missed in the predicted structure  (Figure 5C). This result suggests that CsTegu20.6 can dimerize, confirming that this feature is conserved between the DLCs.