Figures & data
Scheme 1. General scheme for the synthesis of compounds 1–7 and their in vitro Jack bean urease inhibitory activities.
![Scheme 1. General scheme for the synthesis of compounds 1–7 and their in vitro Jack bean urease inhibitory activities.](/cms/asset/3ff2a054-1a08-4f50-a4ec-21abd140d318/ienz_a_294725_f0001_b.gif)
Figure 1. Compound 1 into the active site of urease. The molecule in gray is the ligand with the active site residues. Metals are represented in green.
![Figure 1. Compound 1 into the active site of urease. The molecule in gray is the ligand with the active site residues. Metals are represented in green.](/cms/asset/4189635d-348d-4923-a043-8a22b3143795/ienz_a_294725_f0002_b.gif)
Figure 2. Compound 4 into the active site of urease. The lignad is represented as a ball and stick model.
![Figure 2. Compound 4 into the active site of urease. The lignad is represented as a ball and stick model.](/cms/asset/019e974e-1c05-4058-a5ff-70d1e5622039/ienz_a_294725_f0003_b.gif)
Figure 3. Superimposition of the docking pose of 6a (tan), 6b (gray), 7a (green) 7b (white) showing the difference in the orientation of ring B in the catalytic core of urease. Additionally the active site of urease clearly demonstrating the role of Asp224 and Cys322. The ligands are represented as a ball and stick model.
![Figure 3. Superimposition of the docking pose of 6a (tan), 6b (gray), 7a (green) 7b (white) showing the difference in the orientation of ring B in the catalytic core of urease. Additionally the active site of urease clearly demonstrating the role of Asp224 and Cys322. The ligands are represented as a ball and stick model.](/cms/asset/70966006-f1b4-416a-87c6-a0de75750bd0/ienz_a_294725_f0004_b.gif)