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Molecular docking studies on potent adsorbed receptor of Thrh protein: A new target for biodegradation of indigo dye

Prabhavathi, P.; Rajendran, R.; Sundaram, S. Karthik; Dinesh Kumar, S.; Santhanam, P.; Premnath, D.; Ponmari, G.; Manikandan, A.; Mi-Kyung, Kim


P. Prabhavathi

R. Rajendran

S. Dinesh Kumar

P. Santhanam

D. Premnath

G. Ponmari

A. Manikandan

Kim Mi-Kyung


Vat dyes are aromatic compounds widely used for denim textile industries, this result in a great wastewater problem from this industry due to recalcitrant nature of these dyes. The active protein (ThrH) was purified from Pseudomonas aeruginosa by DEAE-Sepharose A-50 column chromatography and this 3D crystal structure was reported recently. The present study aimed to demonstrate the binding energy between 3D crystal structures of indigo dye and ThrH. We have calculated the gliding score as well as gliding energy based on the hydrophobic interactions between targeted sites (amino acid and dye residue) and the main think is binding energy which was observed maximum level because of the presence of magnesium ions along with catalytic molecules located at the binding sites. The dye degraded mineralized compound was predicted by mass spectrum and infrared spectroscopy.

Journal Article Type Article
Acceptance Date Jun 6, 2016
Online Publication Date Jun 13, 2016
Publication Date Jun 13, 2016
Deposit Date Mar 14, 2023
Publicly Available Date Mar 15, 2023
Publisher OMICS International
Peer Reviewed Peer Reviewed
Volume 7
Issue 4
Keywords Indigo domain, ThrH protein, Binding sites, Induced fit docking (IFD), Schrodinger program


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