5mha
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==D-2-hydroxyacid dehydrogenases (D2-HDH) from Haloferax mediterranei in complex with a mixture of 2-ketohexanoic acid and 2-hydroxyhexanoic acid, and NADPH (1.57 A resolution)== | |
- | + | <StructureSection load='5mha' size='340' side='right' caption='[[5mha]], [[Resolution|resolution]] 1.57Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5mha]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MHA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MHA 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=7N6:(2R)-2-hydroxyhexanoic+acid'>7N6</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
- | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5mh5|5mh5]], [[5mh6|5mh6]]</td></tr> |
- | [[Category: | + | <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=5mha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mha OCA], [http://pdbe.org/5mha PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mha RCSB], [http://www.ebi.ac.uk/pdbsum/5mha PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mha 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> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __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 06:07, 9 May 2018
D-2-hydroxyacid dehydrogenases (D2-HDH) from Haloferax mediterranei in complex with a mixture of 2-ketohexanoic acid and 2-hydroxyhexanoic acid, and NADPH (1.57 A resolution)
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