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Journal:JMB:2

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and  I74  in  particular,  comprises  part  of  PON1's  active-­site  wall.  <scene name='Journal:JMB:2/2d/2'>(D)</scene> Interactions  of  2HQ  with  
and  I74  in  particular,  comprises  part  of  PON1's  active-­site  wall.  <scene name='Journal:JMB:2/2d/2'>(D)</scene> Interactions  of  2HQ  with  
active-­site  residues  (interactions  with  the  catalytic  Ca2+  are  highlighted  in  red).  
active-­site  residues  (interactions  with  the  catalytic  Ca2+  are  highlighted  in  red).  
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<hr/>
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<b>Additional Structures</b>
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<Structure load='Workbench_test3.pdb' size='500' frame='true' align='left' caption='Newly solved structure of rePON1 at pH 6.5' scene='Insert optional scene name here' /><br>
 +
<Structure load='1V04' size='500' frame='true' align='left' caption='Previously solved structure of rePON1 at pH 4.5' scene='Insert optional scene name here' />
<references/>
<references/>
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Revision as of 17:53, 6 March 2012

caption

Drag the structure with the mouse to rotate

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).  

Additional Structures

Newly solved structure of rePON1 at pH 6.5

Drag the structure with the mouse to rotate

Previously solved structure of rePON1 at pH 4.5

Drag the structure with the mouse to rotate
  1. ↑ none yet

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