Gene polymorphisms lead to varied structure and functional properties. A single nucleotide polymorphism (SNP) i.e. Ile105Val (rsl695) in glutathione S-transferase P1 (GSTP1) gene influences cytological toxicity and modulates the risk to occupational diseases. Apart from this, cancer, neuropathy, NOx, SOx and ozone mediated respiratory function decline including lung inflammation, asthma, allergy etc., have been reported in people with this missense mutation. Here, the functional properties of rs1695 polymorph are revisited through a computational approach. Changes incurred by GSTP1 antioxidant protein as a result of alteration in its sequence, have been studied through docking followed by Poisson-Boltzmann electrostatic equation interpretation, grid and coulombic energy profile mapping for protein polymorphs with DelPhi. Molecular docking simulation of variant and wild type (WT) protein was carried out with eight FDA approved compounds that target GSTPI for treatment of various diseases. This was to observe binding pattern variation upon mutation induction. Grid, reaction field and coulombic energy calculation of VVT and mutated polymorph, complexed with and without these moieties was then attempted. Alteration in conformation and energy was observed in apo- and holo- form of GSTPI and their ligand-bound complexes as a result of this mutation. This study is a demo of appraising gene-environment interaction based deleteriousness through molecular docking and dynamics simulation approach. (C) 2017 Elsevier B.V. All rights reserved.