Sandbox 130: Difference between revisions

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<Structure load='4eyl' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here NDN1' />
<Structure load='4eyl' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here NDN1' />
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.
<scene name='37/372730/Asymmetrical_4eyl/2'>TextToBeDisplayed</scene>
<scene name='37/372730/Asymmetrical_4eyl/2'>Asymmetrical Structure NMD1</scene>

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

Wayne Decatur, Student, Meng Han Liu, Allison Granberry