The Zika virus genome encodes three structural proteins (capsid, anterior membrane, and envelope (E)) and seven non-structural proteins (NS1, NS2a, NS2b, NS3, NS4a, NS4b, and NS5) . The envelope protein (E) of the Zika virus (ZIKV) is found on the mature virus's surface. It is responsible for the virus's entrance into cells . Certain sequences of ZIKV glycoprotein envelope (E) resemble the neurotoxic West Nile and Japanese encephalitis viruses. In contrast, other sequences bear a strong resemblance to the dengue virus (DENV) . The flavivirus envelope protein E is a class II virus fusion protein. The fusion process is exceedingly rapid and efficient . As is the case with flaviviruses, the monomeric ZIKV E protein has three distinct domains: the central barrel domain I (DI), the extended dimerization domain II (DII), and the C-terminal immunoglobulin-like domain III (DIII) .Both E and M/prM undergo significant, pH-induced conformational changes during the infection process . Mature virus particles are formed after the host protease furin cleaves prM to remove the pr peptide and expose the fusion loop . After removing the pr peptide in the low pH environment of the endosome, the mature particles subsequently become fused and infected . Protein E's fusion loop (FL) is positioned at the distal end of DII and is composed of hydrophobic residues. FL penetrates endosomal membranes and initiates fusion in response to pH-dependent conformational changes . The E protein is a homodimer that creates an antiparallel herringbone pattern . It has a particular glycosylation loop(12) associated with receptor interaction. Each monomer in the mature flavivirus E protein dimer is related to its neighbors via a two-fold symmetry . The three E protein dimers are parallel to one another in a configuration known as a raft. The virion has a total of 30 rafts . The structure of the ZIKV E protein is transferred from the dimer before fusion to the trimer in the initial state of fusion . The trimer structure of ZIKV E's fusion beginning state is generated utilizing three dimers on the virus's surface and three-fold symmetry . The surface proteins have an icosahedral-like arrangement.