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2glx

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{{Seed}}
 
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[[Image:2glx.png|left|200px]]
 
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<!--
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==Crystal Structure Analysis of bacterial 1,5-AF Reductase==
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The line below this paragraph, containing "STRUCTURE_2glx", creates the "Structure Box" on the page.
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<StructureSection load='2glx' size='340' side='right'caption='[[2glx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2glx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Ensifer_adhaerens Ensifer adhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GLX FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
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{{STRUCTURE_2glx| PDB=2glx | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glx OCA], [https://pdbe.org/2glx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2glx RCSB], [https://www.ebi.ac.uk/pdbsum/2glx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2glx ProSAT]</span></td></tr>
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</table>
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===Crystal Structure Analysis of bacterial 1,5-AF Reductase===
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== Function ==
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[https://www.uniprot.org/uniprot/AFR_ENSAD AFR_ENSAD] Catalyzes the NADPH-specific reduction of 1,5-anhydro-D-fructose to 1,5-anhydro-D-mannitol. Also shows some activity against structurally related compounds such as 3-keto-1,5-anhydro-D-fructose, D-glucosone and D-xylosone. The enzyme cannot use NADH as cosubstrate.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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The line below this paragraph, {{ABSTRACT_PUBMED_16906761}}, adds the Publication Abstract to the page
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Check<jmol>
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(as it appears on PubMed at http://www.pubmed.gov), where 16906761 is the PubMed ID number.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gl/2glx_consurf.spt"</scriptWhenChecked>
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{{ABSTRACT_PUBMED_16906761}}
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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2GLX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ensifer_adhaerens Ensifer adhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2glx ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 A resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis., Dambe TR, Kuhn AM, Brossette T, Giffhorn F, Scheidig AJ, Biochemistry. 2006 Aug 22;45(33):10030-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16906761 16906761]
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</StructureSection>
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Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis., Kuhn A, Yu S, Giffhorn F, Appl Environ Microbiol. 2006 Feb;72(2):1248-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16461673 16461673]
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[[Category: 1,5-anhydro-D-fructose reductase]]
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[[Category: Ensifer adhaerens]]
[[Category: Ensifer adhaerens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dambe, T R.]]
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[[Category: Dambe TR]]
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[[Category: Scheidig, A J.]]
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[[Category: Scheidig AJ]]
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[[Category: 1,5-anhydro-d-fructose]]
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[[Category: 1,5-anhydro-d-mannitol]]
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[[Category: Bacterial 1,5-anhydro-d-fructose reductase]]
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[[Category: Rossmann-fold]]
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[[Category: Sugar metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:01:25 2008''
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Current revision

Crystal Structure Analysis of bacterial 1,5-AF Reductase

PDB ID 2glx

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