User:Cameron Evans/Sandbox 1
From Proteopedia
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'''Glutamate Dehydrogenase''' | '''Glutamate Dehydrogenase''' | ||
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| + | ==Prokaryote== | ||
<applet load='1bgv' size='500' frame='true' align='center' caption='''GluDH of lostridium symbiosum''' /> | <applet load='1bgv' size='500' frame='true' align='center' caption='''GluDH of lostridium symbiosum''' /> | ||
| - | + | = General Structure = | |
| - | + | = 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== |
| + | <applet load='1nr1' size='300' frame='true' align='right' caption='Insert caption here' /> | ||
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| + | ==References== | ||
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<references /> | <references /> | ||
Revision as of 03:33, 1 April 2010
Glutamate Dehydrogenase
Contents |
Prokaryote
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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
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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
