Figure 8

Molecular docking of 3-nitropropionate with native and mutant MtbICL. (A) Structure alignment of docked native and mutant (from last 50 ns simulation) MtbICL was carried out using Chimera 1.10.2. Native and mutant MtbICL are shown in cyan and pink colours respectively. 3-Nitropropionate for native and mutant MtbICL is shown in yellow and red colour respectively. (B) Position of 3-nitropropionate in the binding pocket of the native MtbICL. Structure of 3-nitropropionate is shown in yellow colour and stick form. The residues involved in bonding and non-bonding with 3-nitropropionate are shown in cyan colour. The dashed red lines represent the hydrogen bonding interaction between 3-nitropropionate and amino acid residues- His193 (3.15 Å), Arg228 (3.00 Å) and Asn313 (3.13 Å), Ser315 (3.00 Å) and Thr347 (3.09 Å) from A chain at the catalytic site of native MtbICL. (C) Position of 3-nitropropionate in the binding pocket of the mutant MtbICL. Structure of 3-nitropropionate is shown in red colour and stick form. The residues involved in bonding and non-bonding with 3-nitropropionate are shown in pink colour. The dashed red lines represent the hydrogen bonding interactions between 3-nitropropionate and amino acid residues- Trp93 (2.36 Å) from A chain at the catalytic site of mutant MtbICL.