Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2019 Oct 28;9:15401. doi: 10.1038/s41598-019-51895-2

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Homology model and docking of FabI2, mFabI2 and TCL. (A) Optimized model of FabI2. Alpha-helices flank the parallel β-strands and form an ENR-like architecture. NADH is shown as a stick model. (B) Three-dimensional (3D) view of docked TCL in FabI2. TCL occupies and orients the inhibitory mode in the active site of FabI2. (C) 3D view of molecular interactions of the FabI2-TCL complex. TCL is depicted as magenta stick representation. The phenolic ring of TCL and nicotinamide ring of NADH are stacked by face-to-face weak hydrophobic interactions. The phenolic oxygen of TCL forms an H-bond (green dash) with Y188 of FabI2. (D) Two-dimensional (2D) representation of molecular interactions between FabI2 and TCL. (E) MD optimized model of mFabI2. NADH is shown as stick representation. (F) 3D view of docked TCL in mFabI2. TCL cannot occupy and orient in an inhibitory mode in the active site of mFabI2. TCL is shown as blue stick representation. (G) 3D view of molecular interactions of the mFabI2-TCL complex. The orientation and binding pattern of TCL are completely inverted, where the di-chloro ring of TCL occupies the wide and shallow region of the catalytic cavity of mFabI2. TCL cannot form an H-bond with catalytic residues of mFabI2. TCL is shown as blue stick representation. (H) 2D representation of molecular interactions between mFabI2 and TCL.