Journal:JMB:2
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<applet load="Workbench_test2.pdb" size="500" color="" frame="true" spin="on" Scene ='Journal:JMB:2/Opening/1' align="right" caption=" caption ''"/> | <applet load="Workbench_test2.pdb" size="500" color="" frame="true" spin="on" Scene ='Journal:JMB:2/Opening/1' align="right" caption=" caption ''"/> | ||
| - | === | + | === Catalytic versatility and backups in enzyme active sites: The case of serum paraoxanase 1 === |
| - | <big> | + | <big>Moshe Ben-David, Mikael Elias, Jean-Jacques Filippi, Elisabet Dunach, Israel Silman, Joel Sussman and Dan Tawfik, PhD</big><ref >none yet</ref> |
<hr/> | <hr/> | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
Revision as of 17:14, 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).
- ↑ none yet
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