Sandbox Reserved 644
From Proteopedia
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- | '''Ornithine Transcarbamoylase''' | + | =='''Ornithine Transcarbamoylase'''== |
- | <scene name='Sandbox_Reserved_644/ | + | |
+ | |||
+ | ===='''Structure'''==== | ||
+ | OTC is a trimer. The monomer unit has a CP-binding domain and an amino acid-binding domain. Each of the two discrete substrate-binding domains (SBDs) have an α/β topology with a central β-pleated sheet embedded in flanking α-helices. | ||
+ | The active sites are located at the interface between the protein monomers.<ref>http://en.wikipedia.org/wiki/Ornithine_transcarbamylase</ref> | ||
+ | |||
+ | <scene name='Sandbox_Reserved_644/Active_site/1'>active sites</scene> | ||
+ | |||
+ | References: {{reflist}} |
Revision as of 00:45, 14 November 2012
This Sandbox is Reserved from 30/08/2012, through 01/02/2013 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 636 through Sandbox Reserved 685. |
To get started:
More help: Help:Editing For more help, look at this link: http://proteopedia.org/w/Help:Getting_Started_in_Proteopedia Ornithine TranscarbamoylaseStructureOTC is a trimer. The monomer unit has a CP-binding domain and an amino acid-binding domain. Each of the two discrete substrate-binding domains (SBDs) have an α/β topology with a central β-pleated sheet embedded in flanking α-helices. The active sites are located at the interface between the protein monomers.[1] References: |