2j18

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<StructureSection load='2j18' size='340' side='right'caption='[[2j18]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='2j18' size='340' side='right'caption='[[2j18]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2j18]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldariomyces_fumago Caldariomyces fumago]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J18 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2j18]] 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=2J18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J18 FirstGlance]. <br>
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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=BR:BROMIDE+ION'>BR</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></td></tr>
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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]] 1.75&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=BR:BROMIDE+ION'>BR</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=PRD_900111:2alpha-alpha-mannobiose'>PRD_900111</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cpo|1cpo]], [[2civ|2civ]], [[2ciw|2ciw]], [[2cix|2cix]], [[2ciy|2ciy]], [[2ciz|2ciz]], [[2cj0|2cj0]], [[2cj1|2cj1]], [[2cj2|2cj2]], [[2cpo|2cpo]], [[2j19|2j19]]</div></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/Chloride_peroxidase Chloride peroxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10] </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=2j18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j18 OCA], [https://pdbe.org/2j18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j18 RCSB], [https://www.ebi.ac.uk/pdbsum/2j18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j18 ProSAT]</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=2j18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j18 OCA], [https://pdbe.org/2j18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j18 RCSB], [https://www.ebi.ac.uk/pdbsum/2j18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j18 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Caldariomyces fumago]]
 
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[[Category: Chloride peroxidase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Beitlich, T]]
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[[Category: Leptoxyphium fumago]]
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[[Category: Kuhnel, K]]
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[[Category: Beitlich T]]
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[[Category: Schlichting, I]]
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[[Category: Kuhnel K]]
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[[Category: Schulze-Briese, C]]
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[[Category: Schlichting I]]
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[[Category: Shoeman, R L]]
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[[Category: Schulze-Briese C]]
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[[Category: Chloride]]
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[[Category: Shoeman RL]]
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[[Category: Glycoprotein]]
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[[Category: Heme]]
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[[Category: Iron]]
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[[Category: Manganese]]
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[[Category: Metal-binding]]
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[[Category: Oxidoreductase]]
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[[Category: Peroxidase]]
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[[Category: Pyrrolidone carboxylic acid]]
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Revision as of 14:31, 13 December 2023

Chloroperoxidase mixture of ferric and ferrous states (low dose data set)

PDB ID 2j18

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