5mh6
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==D-2-hydroxyacid dehydrogenases (D2-HDH) from Haloferax mediterranei in complex with 2-ketohexanoic acid and NAD+ (1.35 A resolution)== | |
| + | <StructureSection load='5mh6' size='340' side='right' caption='[[5mh6]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mh6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MH6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MH6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7N5:2-Ketohexanoic+acid'>7N5</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5mh5|5mh5]]</td></tr> | ||
| + | <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=5mh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mh6 OCA], [http://pdbe.org/5mh6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mh6 RCSB], [http://www.ebi.ac.uk/pdbsum/5mh6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mh6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DDH_HALMT DDH_HALMT]] Catalyzes the stereospecific NAD(P)H-dependent reduction of 2-ketocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids. Can use both NADPH or NADH as reductant, displaying a marked preference for NADPH over NADH. Shows a broad substrate specificity, although it displays a marked preference for the 2-ketocarboxylic acids having an unbranched chain of 4-5 carbon atoms.<ref>PMID:17049749</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Cell division protein|Cell division protein]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Baker, P J]] | ||
| + | [[Category: Bisson, C]] | ||
[[Category: Ferrer, J]] | [[Category: Ferrer, J]] | ||
| - | [[Category: | + | [[Category: Harding, S E]] |
| - | [[Category: | + | [[Category: Perez, J Domenech]] |
| - | + | ||
| - | + | ||
[[Category: Pramanpol, N]] | [[Category: Pramanpol, N]] | ||
| + | [[Category: Rice, D W]] | ||
| + | [[Category: Chiral specificity]] | ||
| + | [[Category: D-2-hydroxyacid dehydrogenase]] | ||
| + | [[Category: Halophile]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Reaction mechanism]] | ||
Revision as of 05:47, 6 June 2018
D-2-hydroxyacid dehydrogenases (D2-HDH) from Haloferax mediterranei in complex with 2-ketohexanoic acid and NAD+ (1.35 A resolution)
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