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==Crystal Structure of Human Glycolate Oxidase (GO) in Complex with CDST== | |||
<StructureSection load='2rdt' size='340' side='right'caption='[[2rdt]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2rdt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RDT FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2RD:5-(DODECYLTHIO)-1H-1,2,3-TRIAZOLE-4-CARBOXYLIC+ACID'>2RD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=2rdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rdt OCA], [https://pdbe.org/2rdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rdt RCSB], [https://www.ebi.ac.uk/pdbsum/2rdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rdt ProSAT]</span></td></tr> | ||
[[2rdt]] is a 1 chain structure | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/HAOX1_HUMAN HAOX1_HUMAN] Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids, with high activity towards 2-hydroxy palmitate and 2-hydroxy octanoate. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rd/2rdt_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2rdt ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | ==See Also== | ||
*[[Glycolate oxidase|Glycolate oxidase]] | *[[Glycolate oxidase 3D structures|Glycolate oxidase 3D structures]] | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Holmes RP]] | ||
[[Category: | [[Category: Lowther WT]] | ||
[[Category: | [[Category: Murray MS]] | ||
Latest revision as of 12:21, 21 February 2024
Crystal Structure of Human Glycolate Oxidase (GO) in Complex with CDSTCrystal Structure of Human Glycolate Oxidase (GO) in Complex with CDST
Structural highlights
FunctionHAOX1_HUMAN Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids, with high activity towards 2-hydroxy palmitate and 2-hydroxy octanoate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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