Sandbox Reserved 1665
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
Secondary structure has feature and domains, the N-terminus of the protein contains a central Beta sheet that is surrounded by alpha helices to form the NAD(H)-binding site. Around the C-Terminus end of the protein it consists a mix of alpha/beta domains, which include a catalytic cysteine residue and forms the aldehyde -binding site. The article mentions as well what connects the N and C terminal domains of the protein AldC is by an interdomain linker region. | Secondary structure has feature and domains, the N-terminus of the protein contains a central Beta sheet that is surrounded by alpha helices to form the NAD(H)-binding site. Around the C-Terminus end of the protein it consists a mix of alpha/beta domains, which include a catalytic cysteine residue and forms the aldehyde -binding site. The article mentions as well what connects the N and C terminal domains of the protein AldC is by an interdomain linker region. | ||
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+ | https://proteopedia.org/wiki/images/3/32/Aldehyde_dehydrogenage_of_AldC.PNG | ||
+ | The enzyme functions primarily as a long-chained aliphatic aldehyde dehydrogenase. | ||
== Other important features == | == Other important features == | ||
Revision as of 16:54, 18 April 2021
This Sandbox is Reserved from 01/25/2021 through 04/30/2021 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1665 through Sandbox Reserved 1682. |
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Structure of Aldehyde Dehydrogenase C (AldC) mutant (C291A) from Pseudomonas syringae in complexed with NAD+ and Octanal
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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