Open Access3D Structure of VP1 Structural Protein on Enterovirus A71 Using Swiss-Model
Author(s) -
Suprianto Suprianto,
Made Budiarsa,
Fatmah Dhafir
Publication year - 2020
Publication title -
bioeduscience
Language(s) - English
Resource type - Journals
eISSN - 2614-1558
pISSN - 2614-154X
DOI - 10.29405/j.bes/4137-474353
Subject(s) - ramachandran plot , protein data bank (rcsb pdb) , protein structure , homology modeling , computational biology , structural bioinformatics , structural alignment , protein structure prediction , in silico , uniprot , structural similarity , computer science , biology , sequence alignment , peptide sequence , biochemistry , artificial intelligence , gene , enzyme
Background: VP1 structural protein plays a role as a key player in the pathogenesis, has a uniqueness that is interesting enough to be studied by studying the nature and function of structural proteins VP1. This study aims to predict the three-dimensional structure of proteins VP1 on EV-A71. Methods: The target protein is obtained from UniProt server with an access code A0A097EV89using templates 4cey.1.A (PDB ID) were analyzed in silico by homology method using SWISS-MODEL server. Results: Analysis showed the target protein and the template has 95.29% identity and is composed of 297 amino acids with a value of -2.15 QMEAN. Structural protein VP1 in Ramachandran Plots have a stable structure, non-glycine residue in the outlier regions only around 0.34% (A53 ALA) Rated rotamer outliers 1.61%. Conclusion: The three-dimensional structure model of the protein studied has a stable structure and the information obtained is useful for further research in developing vaccines for diseases caused by EV-A71.