2xvx: Difference between revisions

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<StructureSection load='2xvx' size='340' side='right'caption='[[2xvx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='2xvx' size='340' side='right'caption='[[2xvx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2xvx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Desvh Desvh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XVX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XVX FirstGlance]. <br>
<table><tr><td colspan='2'>[[2xvx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desvh Desvh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XVX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sirohydrochlorin_cobaltochelatase Sirohydrochlorin cobaltochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.3 4.99.1.3] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Sirohydrochlorin_cobaltochelatase Sirohydrochlorin cobaltochelatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.3 4.99.1.3] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2xvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xvx OCA], [http://pdbe.org/2xvx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xvx RCSB], [http://www.ebi.ac.uk/pdbsum/2xvx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xvx 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=2xvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xvx OCA], [https://pdbe.org/2xvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xvx RCSB], [https://www.ebi.ac.uk/pdbsum/2xvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xvx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CBIKP_DESVH CBIKP_DESVH]] Catalyzes the insertion of Co(2+) into sirohydrochlorin. To a lesser extent, is also able to insert Fe(2+) into sirohydrochlorin, yielding siroheme. Its periplasmic location means that it cannot participate in cobalamin biosynthesis and its genomic environment suggests it is likely to be associated with a heme or metal transport system.<ref>PMID:18457416</ref>   
[[https://www.uniprot.org/uniprot/CBIKP_DESVH CBIKP_DESVH]] Catalyzes the insertion of Co(2+) into sirohydrochlorin. To a lesser extent, is also able to insert Fe(2+) into sirohydrochlorin, yielding siroheme. Its periplasmic location means that it cannot participate in cobalamin biosynthesis and its genomic environment suggests it is likely to be associated with a heme or metal transport system.<ref>PMID:18457416</ref>   
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==