1hch: Difference between revisions

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 <StructureSection load='1hch' size='340' side='right'caption='[[1hch]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hch]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HCH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hch]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Armoracia_rusticana Armoracia rusticana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HCH FirstGlance]. <br>
-</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.57&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1atj|1atj]], [[2atj|2atj]], [[3atj|3atj]], [[6atj|6atj]], [[7atj|7atj]]</div></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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] </span></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=1hch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hch OCA], [https://pdbe.org/1hch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hch RCSB], [https://www.ebi.ac.uk/pdbsum/1hch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hch ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PER1A_ARMRU PER1A_ARMRU]] Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
+[https://www.uniprot.org/uniprot/PER1A_ARMRU PER1A_ARMRU] Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1hch ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-A molecular description of oxygen and peroxide activation in biological systems is difficult, because electrons liberated during X-ray data collection reduce the active centres of redox enzymes catalysing these reactions. Here we describe an effective strategy to obtain crystal structures for high-valency redox intermediates and present a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP). We also describe separate experiments in which high-resolution structures could be obtained for all five oxidation states of HRP, showing such structures with preserved redox states for the first time.
-The catalytic pathway of horseradish peroxidase at high resolution.,Berglund GI, Carlsson GH, Smith AT, Szoke H, Henriksen A, Hajdu J Nature. 2002 May 23;417(6887):463-8. PMID:12024218<ref>PMID:12024218</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1hch" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Horseradish peroxidase|Horseradish peroxidase]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
+[[Category: Armoracia rusticana]]
 [[Category: Large Structures]]
-[[Category: Peroxidase]]
+[[Category: Berglund GI]]
-[[Category: Berglund, G I]]
+[[Category: Carlsson GH]]
-[[Category: Carlsson, G H]]
+[[Category: Hajdu J]]
-[[Category: Hajdu, J]]
+[[Category: Henriksen A]]
-[[Category: Henriksen, A]]
+[[Category: Smith AT]]
-[[Category: Smith, A T]]
+[[Category: Szoke H]]
-[[Category: Szoke, H]]
-[[Category: Catalytic intermediate]]
-[[Category: Compound i]]
-[[Category: Horseradish]]
-[[Category: Oxidoreductase]]