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6qka

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Current revision (12:02, 24 January 2024) (edit) (undo)
 
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<StructureSection load='6qka' size='340' side='right'caption='[[6qka]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='6qka' size='340' side='right'caption='[[6qka]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6qka]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QKA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QKA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6qka]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidianus_ambivalens Acidianus ambivalens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QKA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</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]] 2.1&#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=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=TSY:(2S)-2-AMINO-3-TRISULFANYLPROPANOIC+ACID'>TSY</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=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=TSY:(2S)-2-AMINO-3-TRISULFANYLPROPANOIC+ACID'>TSY</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sulfur_oxygenase/reductase Sulfur oxygenase/reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.55 1.13.11.55] </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=6qka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qka OCA], [https://pdbe.org/6qka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qka RCSB], [https://www.ebi.ac.uk/pdbsum/6qka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qka ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6qka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qka OCA], [http://pdbe.org/6qka PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qka RCSB], [http://www.ebi.ac.uk/pdbsum/6qka PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qka ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SOR_ACIAM SOR_ACIAM]] Catalyzes the simultaneous oxidation and reduction of elemental sulfur in the presence of oxygen, with sulfite and hydrogen sulfide as products.<ref>PMID:15030315</ref>
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[https://www.uniprot.org/uniprot/SOR_ACIAM SOR_ACIAM] Catalyzes the simultaneous oxidation and reduction of elemental sulfur in the presence of oxygen, with sulfite and hydrogen sulfide as products.<ref>PMID:15030315</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Numerous microorganisms oxidize sulfur for energy conservation and contribute to the global biogeochemical sulfur cycle. We have determined the 1.7 angstrom-resolution structure of the sulfur oxygenase reductase from the thermoacidophilic archaeon Acidianus ambivalens, which catalyzes an oxygen-dependent disproportionation of elemental sulfur. Twenty-four monomers form a large hollow sphere enclosing a positively charged nanocompartment. Apolar channels provide access for linear sulfur species. A cysteine persulfide and a low-potential mononuclear non-heme iron site ligated by a 2-His-1-carboxylate facial triad in a pocket of each subunit constitute the active sites, accessible from the inside of the sphere. The iron is likely the site of both sulfur oxidation and sulfur reduction.
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X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme.,Urich T, Gomes CM, Kletzin A, Frazao C Science. 2006 Feb 17;311(5763):996-1000. PMID:16484493<ref>PMID:16484493</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6qka" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acidianus ambivalens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Sulfur oxygenase/reductase]]
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[[Category: Frazao C]]
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[[Category: Frazao, C]]
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[[Category: Klezin A]]
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[[Category: Klezin, A]]
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[[Category: Poell U]]
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[[Category: Poell, U]]
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[[Category: 2-his-1-carboxylate facial triad]]
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[[Category: Biogeochemical sulfur cycle]]
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[[Category: Cysteine persulphuration]]
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[[Category: Oxidoreductase]]
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[[Category: Sulfur oxygenase reductase]]
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Current revision

Di-tert-butyl Polysulfide inhibited sulfur oxygenase reductase

PDB ID 6qka

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