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An in-silico analysis showing the interaction of FAD ligand with cytokinin dehydrogenase enzyme and with its domain part in rice | Swain | Computational Molecular Biology

An in-silico analysis showing the interaction of FAD ligand with cytokinin dehydrogenase enzyme and with its domain part in rice  

Pranati Swain , Lambodar Behera
Central rice research institute, India
Author    Correspondence author
Computational Molecular Biology, 2014, Vol. 4, No. 15   doi: 10.5376/cmb.2014.04.0015
Received: 10 Dec., 2014    Accepted: 26 Dec., 2014    Published: 30 Dec., 2014
© 2014 BioPublisher Publishing Platform
This is an open access article published under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Preferred citation for this article:

Swain and Behera, 2014, An in-silico analysis showing the interaction of FAD ligand with cytokinin dehydrogenase enzyme and with its domain part in rice, Computational Molecular Biology, Vol.4, No.15, 1-5 (doi: 10.5376/cmb.2014.04.0015)

Abstract

The cytokinin dehydrogenase enzyme plays an important role in the high grain production of rice. This enzyme interacts with the FAD ligand. This study shows the domain region of the enzyme which was identified by protparam tool, generated homology models using modeller9.12 tool, models were validated using errat, procheck saves server, prosa and anolea server. Then the active sites were predicted by using castP server. Finally the interaction was studied between the FAD and cytokinin dehydrogenase and with its domain part. The stronger interaction was found between the FAD and the domain of the cytokinin degydrogenase with the binding enegy of -10.91. ALA6, ARG1, AR536, TYR10, ASP55, ALA57, CYS38 of FAD is binding to the domain part of cytokinin degydrogenase in rice.

Keywords
FAD Ligand; Cytokinin dehydrogenase enzyme; Interaction between ligand and enzyme; Functional domain
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