Sandbox 130: Difference between revisions
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The active site contains key features for hydrolyzing carbapenems: | The active site contains key features for hydrolyzing carbapenems: | ||
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 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/ | Zinc ion 2 (<scene name='37/372730/Symmetrical_4eyl_zn2/3'>Zn2</scene>) is coordinated by three residues: H250, C208, and D124. | ||
Revision as of 21:52, 20 July 2016
New Delhi Metallo-β-LactamaseNew Delhi Metallo-β-Lactamase
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The New Delhi metallo-β-lactamase () in complex with meropenem () demonstrates the mechanism in which the active site binds and hydrolyzed the a carbapenem, in this case meropenem. 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:
Zinc ion 1() is coordinated by three histidine residues: H120, H122 and H189. Zinc ion 2 () is coordinated by three residues: H250, C208, and D124.