User:Cameron Evans/Sandbox 1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(→Specificity)
Line 11: Line 11:
===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 prokaryotic GluDH</scene> is made up of polar interactions from K89 and S380 and hydrophobic interactions from G90, V377 and A163. The last three residues that make this interaction are highly conserved among amino acid dehydrogenases. <ref name="1bgv">PMID:8263917</ref>
 +
The polar residues make specific contacts with the glutamine substrate.
==Eukaryote==
==Eukaryote==

Revision as of 03:48, 1 April 2010

Glutamate Dehydrogenase



Contents

Prokaryote

PDB ID 1bgv

Drag the structure with the mouse to rotate

General Structure

Specificity

is made up of polar interactions from K89 and S380 and hydrophobic interactions from G90, V377 and A163. The last three residues that make this interaction are highly conserved among amino acid dehydrogenases. [1] The polar residues make specific contacts with the glutamine substrate.

Eukaryote

Insert caption here

Drag the structure with the mouse to rotate



References

  1. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Cameron Evans

Retrieved from "http://52.214.119.220/wiki/index.php/User:Cameron_Evans/Sandbox_1"
Personal tools