6itk: Difference between revisions

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-'''Unreleased structure'''
-The entry 6itk is ON HOLD  until Paper Publication
+==Crystal strcuture of malate dehydrogenase from Corynebacterium glutamicum ATCC 13032 in complex with NAD and malate==
+<StructureSection load='6itk' size='340' side='right'caption='[[6itk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-Authors: Seo, H., Kim, K.-J.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6itk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ITK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ITK FirstGlance]. <br>
-Description: Crystal strcuture of malate dehydrogenase from Corynebacterium glutamicum ATCC 13032 in complex with NAD and malate
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LMR:(2S)-2-HYDROXYBUTANEDIOIC+ACID'>LMR</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </span></td></tr>
-[[Category: Kim, K.-J]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6itk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6itk OCA], [http://pdbe.org/6itk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6itk RCSB], [http://www.ebi.ac.uk/pdbsum/6itk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6itk ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/MDH_CORGL MDH_CORGL]] Catalyzes the reversible oxidation of malate to oxaloacetate. Exhibits higher catalytic efficiency for oxaloacetate reduction than for malate oxidation in vitro. Almost equally active both for NADH and NADPH on the bases of the kcat values at pH 6.5, but catalytic efficiency for oxaloacetate reduction is 50-fold higher with NADH.<ref>PMID:16233457</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Malate dehydrogenase]]
+[[Category: Kim, K J]]
 [[Category: Seo, H]]
+[[Category: Dehydrogenase]]
+[[Category: Oxidoreductase]]