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Sandbox GGC13
From Proteopedia
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The active site contains three different binding pockets to accommodate the substrate, Nicotinamide, and adenine. | The active site contains three different binding pockets to accommodate the substrate, Nicotinamide, and adenine. | ||
The substrate binding pocket relies on heavily on hydrogen binding and ionic interactions in order to effectively bind the substrate. Upon substrate binding, the substrate binding pocket undergoes a conformation change where interactions between the substrate or inhibitor and a glutamine residue (Q99) essentially pull the active loop closed. | The substrate binding pocket relies on heavily on hydrogen binding and ionic interactions in order to effectively bind the substrate. Upon substrate binding, the substrate binding pocket undergoes a conformation change where interactions between the substrate or inhibitor and a glutamine residue (Q99) essentially pull the active loop closed. | ||
| - | <scene name='78/781197/Oxamate/ | + | <scene name='78/781197/Oxamate/3'>Close up interactions between the substrate binding pocket and the inhibitor, oxamate. The substrate active site to which oxamate is bound is in the closed conformation.</scene> |
<scene name='78/781197/Nadh/1'>Close up interactions between the NADH and adenine binding pockets and the cofactor, NADH.</scene> | <scene name='78/781197/Nadh/1'>Close up interactions between the NADH and adenine binding pockets and the cofactor, NADH.</scene> | ||
Revision as of 00:50, 22 April 2018
Crystal Structure of Lactate Dehydrogenase A
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
