Sandbox 130: Difference between revisions

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Zn1 (coordinated by three histidine residues), acts as a major constituent of oxyanion hole to stabilize tetrahedral intermediate. It also acts as a Lewis acid for interaction with lactam carbonyl in Michaelis complex and acts to suppress the pKa of the hyrdolytic water to (~5-6) to facilitate it's nucleophilic role.
Zn1 (coordinated by three histidine residues), acts as a major constituent of oxyanion hole to stabilize tetrahedral intermediate. It also acts as a Lewis acid for interaction with lactam carbonyl in Michaelis complex and acts to suppress the pKa of the hyrdolytic water to (~5-6) to facilitate it's nucleophilic role.
The active site contains key features for hydrolyzing carbapenems:  
The active site contains key features for hydrolyzing carbapenems:  
   Zinc ion 1(Zn1) is coordinated by three histidine residues: H120, H122 and H189.  
   Zinc ion 1(<scene name='37/372730/Chaina_cornflowerblue_zn1/1'>Zn1</scene>) is coordinated by three histidine residues: H120, H122 and H189.  
   Zinc ion 2 (<scene name='37/372730/Symmetrical_4eyl_zn2/1'>Zn2</scene>) is coordinated by three residues: H250, C208, and D124.
   Zinc ion 2 (<scene name='37/372730/Symmetrical_4eyl_zn2/1'>Zn2</scene>) is coordinated by three residues: H250, C208, and D124.

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Wayne Decatur, Student, Meng Han Liu, Allison Granberry