1996-2019. All Rights Reserved. Online Journal of Bioinformatics . You may not store these pages in any form except for your own personal use. All other usage or distribution is illegal under international copyright treaties. Permission to use any of these pages in any other way besides the  before mentioned must be gained in writing from the publisher. This article is exclusively copyrighted in its entirety to OJB publications. This article may be copied once but may not be, reproduced or  re-transmitted without the express permission of the editors. This journal satisfies the refereeing requirements (DEST) for the Higher Education Research Data Collection (Australia). Linking: To link to this page or any pages linking to this page you must link directly to this page only here rather than put up your own page.


Online Journal of Bioinformatics 

Volume 17(2):105-115, 2016.

Molecular docking imidazo[1,2-b]pyridazines on methicillin resistant Staphylococcus aureus.


Raman PK, Murali Krishna K, Ramana PV.


Department of Chemistry, Sri Krishnadevaraya University, Ananthapuramu 515 003. A.P., India




Raman PK, Murali Krishna K, Ramana PV*., Molecular docking imidazo[1,2-b]pyridazine heterocyclics on methicillin resistant Staphylococcus aureus, Onl J Bioinform., 17(2):105-115, 2016. In silico binding affinity of a 3D Penicillin binding protein (PBP2a) inhibitor from Staphylococcus aureus using GOLD scoring fitness is described. Amino acid residues SER 112, PRO 113, THR 115, TYR 116 and GLY 121 in PBP2a were involved in inhibition due to hydrogen bonding interactions and stability of the target-ligand complex. Docking results simulated in vitro anti-microbial activity of analogues forming 5 hydrogen bonds. In the binding pocket, common H-bonding interactions were formed between all docked drugs and GLY 121, TYR 122, LYS 123, ALA 137. Strong H-bonding interactions between the hydroxyl group (H12) of analogue and an oxygen atom of GLU31 and another hydrogen bond between hydroxyl group (H11) and oxygen atom of ASP111 was found. Two H-bonding interactions were formed between oxygen atom of 5-FU, ASP29 and CYS 44 of PBP2a. Binding orientation of compounds in the PBP2a of MRSA binding pocket may inhibit of enzyme activity. One compound (4) may exhibit strong inhibitory effect on PBP2a. Binding-docking is illustrated graphically


Keywords: Docking, In silico Pencillin binding protein, imidazo[1,2-b]pyridazine based heterocyclics. Methicillin Resistant Staphylococcus aureus.