<?xml version="1.0" encoding="utf-8"?>
<Journal>
<Journal-Info>
<name>International Journal of Pharma and Bio Sciences</name>
<website>ijpbs.net</website>
<email>editorijpbs@rediffmail.com (or) editorofijpbs@yahoo.com (or) prasmol@rediffmail.com</email>
</Journal-Info>
<article>
<article-id pub-id-type='other'>10.22376/ijpbs.2019.10.1.p1-12</article-id>
<issue_number>Volume 3 Issue 3</issue_number>
<issue_period>2012 (July - September)</issue_period>
<title>In Silico Studies of Nifh Protein Structure And its Post – Translational Modification in Bradyrhizobium Sp. Ors278. </title>
<abstract> lessThan i greaterThan Bradyrhizobium lessThan /i greaterThan  is a gram negative, symbiotic nitrogen fixer that can form nodules in the roots of leguminous plants. The enzyme nitrogenase is the utmost important component of nitrogen fixing machinery, comprising two proteins, a molydenum-iron protein (MoFe protein) and an iron protein (Fe protein). Since, there is no comprehensive data on the tertiary structure of the nitrogenase iron protein (NifH) of  lessThan i greaterThan Bradyrhizobium lessThan /i greaterThan  sp. ORS278 in the public domain, we decided to construct a three dimensional structure of the protein based on homology modeling technique. The model was constructed using the crystal structure of the NifH protein (1NIP) from  lessThan i greaterThan Azotobacter vinelandii lessThan /i greaterThan  as a template. The functionally important regions of the protein and position of 4Fe-4S cluster in the protein were investigated. The 3D model was further utilized to highlight the importance of covalent modification site (Arg-102) in post-translational regulation of the nitrogenase enzyme through  lessThan i greaterThan in-silico lessThan /i greaterThan  docking experiment.</abstract>
<authors>Subarna takur, asim k Bothra And Arnab Sen</authors>
<keywords>Bradyrhizobium, symbiotic, homology modeling, template, docking.</keywords>
<pages>22-32</pages>
</article>
</Journal>
