6itk: Difference between revisions
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<StructureSection load='6itk' size='340' side='right'caption='[[6itk]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='6itk' size='340' side='right'caption='[[6itk]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6itk]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6itk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum_ATCC_13032 Corynebacterium glutamicum ATCC 13032]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6ITK FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMR:(2S)-2-HYDROXYBUTANEDIOIC+ACID'>LMR</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6itk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6itk OCA], [https://pdbe.org/6itk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6itk RCSB], [https://www.ebi.ac.uk/pdbsum/6itk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6itk ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Corynebacterium glutamicum ATCC 13032]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kim K-J]] | |||
[[Category: Kim | [[Category: Seo H]] | ||
[[Category: Seo | |||