Mucormycosis is an invasive fungal infection with considerably high mortality rates in immunocompromised individuals. Due to COVID-19 pandemic, the disease has resurfaced recently and lack of appropriate antifungals resulted in a poor outcome in patients. The iron uptake mechanism in Rhizopus delemar, the predominant causal agent is crucial for its survival and pathogenesis in human host. The current study focuses on the structural dynamics of high affinity iron permease (Ftr1) which act as a virulence factor in this fatal fungal disease. Ftr1 is a transmembrane protein which is responsible for the transport of Fe ³⁺ ion from the extracellular milieu to the cytoplasm under iron-starving conditions in Rhizopus. In this work, the three-dimensional modelling of Ftr1 was carried out and it was found to possess seven transmembrane helices with N-terminal lying in the extracellular region and C-terminal in the intracellular region. Moreover, the present study delineates the interaction of glutamic acid residues, found in the REGLE motif of the fourth transmembrane helix with Fe ³⁺. The molecular dynamics (MD) simulation study revealed that the glycine present in the motif destabilizes the helix thereby bringing E157 closer to the positively charged ion. Understanding the interaction between Fe ³⁺ ion and Ftr1 would be helpful in designing effective small molecule drugs against this novel therapeutic target for treating mucormycosis.