1mj4: Difference between revisions

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<StructureSection load='1mj4' size='340' side='right'caption='[[1mj4]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
<StructureSection load='1mj4' size='340' side='right'caption='[[1mj4]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mj4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MJ4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mj4]] 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=1MJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MJ4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.2&#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;'>[[1sox|1sox]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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'>[https://en.wikipedia.org/wiki/Sulfite_oxidase Sulfite oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.1 1.8.3.1] </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=1mj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mj4 OCA], [https://pdbe.org/1mj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mj4 RCSB], [https://www.ebi.ac.uk/pdbsum/1mj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mj4 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=1mj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mj4 OCA], [https://pdbe.org/1mj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mj4 RCSB], [https://www.ebi.ac.uk/pdbsum/1mj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mj4 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[https://www.uniprot.org/uniprot/SUOX_HUMAN SUOX_HUMAN]] Defects in SUOX are the cause of isolated sulfite oxidase deficiency (ISOD) [MIM:[https://omim.org/entry/272300 272300]]; also known as sulfocysteinuria. ISOD is characterized by neurological abnormalities including multicystic leukoencephalopathy with brain atrophy. Patients often suffer from seizures. Often leads to death at an early age.<ref>PMID:9428520</ref> <ref>PMID:9600976</ref> <ref>PMID:10519592</ref> <ref>PMID:12112661</ref> <ref>PMID:12368985</ref>
[https://www.uniprot.org/uniprot/SUOX_HUMAN SUOX_HUMAN] Defects in SUOX are the cause of isolated sulfite oxidase deficiency (ISOD) [MIM:[https://omim.org/entry/272300 272300]; also known as sulfocysteinuria. ISOD is characterized by neurological abnormalities including multicystic leukoencephalopathy with brain atrophy. Patients often suffer from seizures. Often leads to death at an early age.<ref>PMID:9428520</ref> <ref>PMID:9600976</ref> <ref>PMID:10519592</ref> <ref>PMID:12112661</ref> <ref>PMID:12368985</ref>  
== Function ==
[https://www.uniprot.org/uniprot/SUOX_HUMAN SUOX_HUMAN]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[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=1mj4 ConSurf].
</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=1mj4 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The molybdenum- and iron-containing enzyme sulfite oxidase catalyzes the physiologically vital oxidation of sulfite to sulfate. Sulfite oxidase contains three domains: an N-terminal cytochrome b(5) domain, a central domain harboring the molybdenum cofactor (Moco) and a C-terminal dimerization domain. Oxidation of the substrate sulfite is coupled to the transfer of two electrons to the molybdenum cofactor. Subsequently, these electrons are passed on, one at a time, to the b(5) heme of sulfite oxidase and from there to the soluble electron carrier cytochrome c. The crystal structure of the oxidized human sulfite oxidase cytochrome b(5) domain has been determined at 1.2 A resolution and has been refined to a crystallographic R factor of 0.107 (R(free) = 0.137). A comparison of this structure with other b(5)-type cytochromes reveals distinct structural features present in the sulfite oxidase b(5) domain which promote optimal electron transport between the Moco of sulfite oxidase and the heme of cytochrome c.
The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain.,Rudolph MJ, Johnson JL, Rajagopalan KV, Kisker C Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1183-91. Epub 2003, Jun 27. PMID:12832761<ref>PMID:12832761</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mj4" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sulfite oxidase]]
[[Category: Johnson JL]]
[[Category: Johnson, J L]]
[[Category: Kisker C]]
[[Category: Kisker, C]]
[[Category: Rajagopalan KV]]
[[Category: Rajagopalan, K V]]
[[Category: Rudolph MJ]]
[[Category: Rudolph, M J]]
[[Category: Cytochrome b5]]
[[Category: Heme]]
[[Category: Oxidoreductase]]
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