1.3.1.118	crystallization and structure determination of InhA ternary complexes with PT501, PT504, PT506, PT511, PT512 and PT514	748042	
1.3.1.118	crystallization of InhA with isoniazid-NADP bound and the structure of the complex is solved	748020	
1.3.1.118	hanging drop vapor diffusion technique, formation of the ternary enzyme/NAD+x012-(o-tolyloxy)-5-hexylphenol complex	748167	
1.3.1.118	molecular docking studies are performed on the crystal structure of Mycobacterium tuberculosis enoyl reductase (InhA) complexed with 1-cyclohexyl-N-(3,5-dichlorophenyl)-5-oxopyrrolidine-3-carboxamide	747250	
1.3.1.118	overview of 80 available crystal structures of wild-type and mutant InhA, in its apo form, in complex with its cofactor, with an analogue of its natural ligands (C16 fatty acid and/or NADH) or with inhibitor	747697	
1.3.1.118	the crystal structure of the enzyme in complex with NAD+ and trans-2-hexadecenoyl-(N-acetylcysteamine)-thioester reveals that the substrate binds in a general U-shaped conformation, with the trans double bond positioned directly adjacent to the nicotinamide ring of NAD+. The side chain of Tyr158 directly interacts with the thioester carbonyl oxygen of the C16 fatty acyl substrate and therefore can help stabilize the enolate intermediate, proposed to form during substrate catalysis. Hydrophobic residues, primarily from the substrate binding loop (residues 196-219), engulf the fatty acyl chain portion of the substrate. The substrate binding loop of InhA is longer than that of other enoyl-ACP reductases and creates a deeper substrate binding crevice, consistent with the ability of InhA to recognize longer chain fatty acyl substrates	748146	
1.3.1.118	the crystal structure of the enzyme in complex with the inhibitor N-(4-methylbenzoyl)-4-benzylpiperidine reveals the binding mode of the inhibitor within the active site	747251