Sandbox 130: Difference between revisions
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The New Delhi metallo-β-lactamase (<scene name='37/372730/Asymmetrical_4eyl/2'>NMD-1</scene>) in complex with meropenem (<scene name='37/372730/Symmetrical_4eyl/1'>Chain A</scene>) demonstrates the mechanism in which the active site binds and hydrolyzed the a carbapenem, in this case meropenem. | The New Delhi metallo-β-lactamase (<scene name='37/372730/Asymmetrical_4eyl/2'>NMD-1</scene>) in complex with meropenem (<scene name='37/372730/Symmetrical_4eyl/1'>Chain A</scene>) 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. | 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(Zn1) 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. | |||