2glx

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==Crystal Structure Analysis of bacterial 1,5-AF Reductase==
==Crystal Structure Analysis of bacterial 1,5-AF Reductase==
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<StructureSection load='2glx' size='340' side='right' caption='[[2glx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='2glx' size='340' side='right'caption='[[2glx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2glx]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33212 Atcc 33212]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GLX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2glx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_33212 Atcc 33212]. 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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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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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</td></tr><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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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">afr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106592 ATCC 33212])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">afr ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106592 ATCC 33212])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,5-anhydro-D-fructose_reductase 1,5-anhydro-D-fructose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.263 1.1.1.263] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/1,5-anhydro-D-fructose_reductase 1,5-anhydro-D-fructose reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.263 1.1.1.263] </span></td></tr>
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<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=2glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glx OCA], [http://pdbe.org/2glx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2glx RCSB], [http://www.ebi.ac.uk/pdbsum/2glx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2glx ProSAT]</span></td></tr>
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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>
</table>
</table>
== Function ==
== Function ==
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[[http://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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[[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gl/2glx_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: 1,5-anhydro-D-fructose reductase]]
[[Category: 1,5-anhydro-D-fructose reductase]]
[[Category: Atcc 33212]]
[[Category: Atcc 33212]]
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[[Category: Large Structures]]
[[Category: Dambe, T R]]
[[Category: Dambe, T R]]
[[Category: Scheidig, A J]]
[[Category: Scheidig, A J]]

Revision as of 19:09, 10 March 2021

Crystal Structure Analysis of bacterial 1,5-AF Reductase

PDB ID 2glx

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