2j5m: Difference between revisions

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-[[Image:2j5m.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2j5m", creates the "Structure Box" on the page.
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-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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-{{STRUCTURE_2j5m|  PDB=2j5m  |  SCENE=  }}
-'''STRUCTURE OF CHLOROPEROXIDASE COMPOUND 0'''
+==Structure of Chloroperoxidase Compound 0==
+<StructureSection load='2j5m' size='340' side='right'caption='[[2j5m]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2j5m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptoxyphium_fumago Leptoxyphium fumago]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J5M 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]] 1.75&#8491;</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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene>, <scene name='pdbligand=PRD_900111:2alpha-alpha-mannobiose'>PRD_900111</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=2j5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j5m OCA], [https://pdbe.org/2j5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j5m RCSB], [https://www.ebi.ac.uk/pdbsum/2j5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j5m ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PRXC_LEPFU PRXC_LEPFU] Catalyzes peroxidative halogenations involved in the biosynthesis of clardariomycin (2,2-dichloro-1,3-cyclo-pentenedione). The enzyme also has potent catalase activity and in the absence of halide ion, acts as a peroxidase similar to plant peroxidases.
+== 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/j5/2j5m_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=2j5m ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We have determined the crystal structure of the chloroperoxidase (CPO) hydroperoxo reaction intermediate (CPO compound 0) at 1.75-A resolution. The intermediate was generated through controlled photoreduction of the CPO oxygen complex during x-ray data collection, which was monitored by recording of the crystal absorption spectra. Initially, the peroxo-anion species was formed and then protonated to yield compound 0. Quantum chemical calculations indicate that the peroxo-anion species is not stable and collapses instantaneously to compound 0. Compound 0 is present in the ferric low-spin doublet ground state and is characterized by a long O O bond length of 1.5 A and a Fe O bond distance of 1.8 A, which is also observed in the crystal structure.
-==Overview==
+Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes.,Kuhnel K, Derat E, Terner J, Shaik S, Schlichting I Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):99-104. Epub 2006 Dec 26. PMID:17190816<ref>PMID:17190816</ref>
-We have determined the crystal structure of the chloroperoxidase (CPO) hydroperoxo reaction intermediate (CPO compound 0) at 1.75-A resolution. The intermediate was generated through controlled photoreduction of the CPO oxygen complex during x-ray data collection, which was monitored by recording of the crystal absorption spectra. Initially, the peroxo-anion species was formed and then protonated to yield compound 0. Quantum chemical calculations indicate that the peroxo-anion species is not stable and collapses instantaneously to compound 0. Compound 0 is present in the ferric low-spin doublet ground state and is characterized by a long O O bond length of 1.5 A and a Fe O bond distance of 1.8 A, which is also observed in the crystal structure.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-J5M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Leptoxyphium_fumago Leptoxyphium fumago]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J5M OCA].
+</div>
+<div class="pdbe-citations 2j5m" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes., Kuhnel K, Derat E, Terner J, Shaik S, Schlichting I, Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):99-104. Epub 2006 Dec 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17190816 17190816]
+*[[Haloperoxidase|Haloperoxidase]]
-[[Category: Chloride peroxidase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Leptoxyphium fumago]]
-[[Category: Single protein]]
+[[Category: Derat E]]
-[[Category: Derat, E.]]
+[[Category: Kuhnel K]]
-[[Category: Kuhnel, K.]]
+[[Category: Schlichting I]]
-[[Category: Schlichting, I.]]
+[[Category: Shaik S]]
-[[Category: Shaik, S.]]
+[[Category: Terner J]]
-[[Category: Terner, J.]]
-[[Category: Chloride]]
-[[Category: Glycoprotein]]
-[[Category: Heme]]
-[[Category: Iron]]
-[[Category: Manganese]]
-[[Category: Metal-binding]]
-[[Category: Oxidoreductase]]
-[[Category: Peroxidase]]
-[[Category: Pyrrolidone carboxylic acid]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 08:22:33 2008''