Homology modeling is a very useful and essential technique for determining protein tertiary structure using known protein or template structure and amino acid sequence data. However, if the sequence identity is below 30%, the model will not provide suitable efficiency in structure determination . After searching for suitable templates in the PDB database using BLASTp, 10 non-homologous proteins out of 20 EHPs showed sequence identity greater than 30% (Table ). Therefore, those 10 EHPs were used to build tertiary structures using two different servers, such as SWISS-MODEL and Phyre2. After generating the models, PROCHECK Ramachandran plot showed residues in the most favored regions ≥ 90% for only five proteins generated by SWISS-MODEL and for only three proteins generated by Phyre2. In the Verify3D test, four proteins from SWISS-MODEL passed the test whereas only one protein from Phyre2 passed the test. Similar trend was observed in the ERRAT server test. Therefore, SWISS-MODEL was found to be more efficient than Phyre2 according to the quality assessment results. Therefore, the PDB files for all the proteins generated by SWISS-MODEL were further submitted to the GalaxyRefine server for model refinement.