Journal:JMB:2
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<table width='1000' align='center' cellpadding='2'><td rowspan='2'> </td><td bgcolor='#eeeeee'> | <table width='1000' align='center' cellpadding='2'><td rowspan='2'> </td><td bgcolor='#eeeeee'> | ||
| - | <center>'''rePON1 with 2HQ''' </center><applet load='Workbench_test2.pdb' size='325' frame='true' align='left' scene= | + | <center>'''rePON1 with 2HQ''' </center><applet load='Workbench_test2.pdb' size='325' frame='true' align='left' scene='Journal:JMB:2/Opening/1' target='0' /></td><td bgcolor='#eeeeee'> |
| - | <center>'''rePON1 at pH of 6.5''' </center><applet load='Workbench_test3.pdb' size='325' frame='true' align='center' scene= | + | <center>'''rePON1 at pH of 6.5''' </center><applet load='Workbench_test3.pdb' size='325' frame='true' align='center' scene='Journal:JMB:2/New_no_hq/2' target='0' /></td><td bgcolor='#eeeeee'> |
<center>'''rePON1 at pH of 4.5''' </center><applet load='1V04' size='325' frame='true' align='right' scene="" target='0' /></td><td bgcolor='#eeeeee'> | <center>'''rePON1 at pH of 4.5''' </center><applet load='1V04' size='325' frame='true' align='right' scene="" target='0' /></td><td bgcolor='#eeeeee'> | ||
<references/> | <references/> | ||
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Revision as of 18:51, 6 March 2012
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Catalytic versatility and backups in enzyme active sites: The case of serum paraoxanase 1
Moshe Ben-David, Mikael Elias, Jean-Jacques Filippi, Elisabet Dunach, Israel Silman, Joel Sussman and Dan Tawfik, PhD[1]
Molecular Tour
Figure 2. Structural details of the 2HQ/rePON1 complex at pH 6.5; 2HQ and the structured active-site loop in the rePON1-2HQ complex structure. Overlay of the phosphate ion in the apo rePON1 at pH 6.5 and of 2HQ in the rePON1-2HQ complex. The first segment of the active-site loop, and residues Y71 and I74 in particular, comprises part of PON1's active-site wall. Interactions of 2HQ with active-site residues (interactions with the catalytic Ca2+ are highlighted in red).
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