User:Cameron Evans/Sandbox 1
From Proteopedia
(Difference between revisions)
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==Prokaryote== | ==Prokaryote== | ||
| - | <applet load='1bgv' size=' | + | <applet load='1bgv' size='300' frame='true' align='center' caption='''GluDH of lostridium symbiosum''' /> |
| - | = General Structure = | + | ===General Structure=== |
| - | = Specificity = | + | ===Specificity=== |
<scene name='User:Cameron_Evans/Sandbox_1/1bgv_spec_pocket/2'>The Specificity pocket of 1bgv</scene> is made up of polar interactions from K89 and S380 and hydrophobic interactions from G90, V377 and A163. <ref name="1bgv">PMID:8263917</ref> The polar residues... | <scene name='User:Cameron_Evans/Sandbox_1/1bgv_spec_pocket/2'>The Specificity pocket of 1bgv</scene> is made up of polar interactions from K89 and S380 and hydrophobic interactions from G90, V377 and A163. <ref name="1bgv">PMID:8263917</ref> The polar residues... | ||
==Eukaryote== | ==Eukaryote== | ||
| - | <applet load='1nr1' size='300' frame='true' align=' | + | <applet load='1nr1' size='300' frame='true' align='center' caption='Insert caption here' /> |
Revision as of 03:35, 1 April 2010
Glutamate Dehydrogenase
Contents |
Prokaryote
|
General Structure
Specificity
is made up of polar interactions from K89 and S380 and hydrophobic interactions from G90, V377 and A163. [1] The polar residues...
Eukaryote
|
References
- ↑ Stillman TJ, Baker PJ, Britton KL, Rice DW. Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. J Mol Biol. 1993 Dec 20;234(4):1131-9. PMID:8263917 doi:http://dx.doi.org/10.1006/jmbi.1993.1665
