National Academy of Agricultural Sciences (NAAS)
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PRINT ISSN : 2319-7692
Online ISSN : 2319-7706 Issues : 12 per year Publisher : Excellent Publishers Email : editorijcmas@gmail.com / submit@ijcmas.com Editor-in-chief: Dr.M.Prakash Index Copernicus ICV 2018: 95.39 NAAS RATING 2020: 5.38 |
Glyoxalase I (gly I) and Glyoxalase II (gly II), zinc-binding enzymes of the glyoxalase pathway, carry out catabolism of methylglyoxal (MG). Gly II gene cloned from Oryza sativa has been widely used in genetic transformation experiments for salinity tolerance. In the present study, we tried to propose a potential model of the Oryza sativa gly II protein generated via SWISS-MODEL, CPH models 3.0 Server, I-TASSER, HHPred and MODELLER software. Thirteen different models were constructed using different tools and were further optimized by performing Energy minimization and Loop building techniques. The final model was suggested after analyzing and validating the structure by using Structural Analysis and Verification Server (SAVS). Further functional characterization of the modeled protein was accomplished by tool COFACTOR which involves prediction of functional active site region and binding site region. This model can be used for further analysis for different studies.
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