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6efv

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==The NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation that is unique to this diflavin reductase==
==The NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation that is unique to this diflavin reductase==
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<StructureSection load='6efv' size='340' side='right' caption='[[6efv]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
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<StructureSection load='6efv' size='340' side='right'caption='[[6efv]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6efv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EFV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EFV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6efv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EFV 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=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.341&#8491;</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/Sulfite_reductase_(NADPH) Sulfite reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.2 1.8.1.2] </span></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=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6efv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6efv OCA], [http://pdbe.org/6efv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6efv RCSB], [http://www.ebi.ac.uk/pdbsum/6efv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6efv ProSAT]</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=6efv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6efv OCA], [https://pdbe.org/6efv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6efv RCSB], [https://www.ebi.ac.uk/pdbsum/6efv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6efv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/W8SX42_ECOLX W8SX42_ECOLX]] Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.[HAMAP-Rule:MF_01541][PIRNR:PIRNR000207][SAAS:SAAS00040600]
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[https://www.uniprot.org/uniprot/W8SX42_ECOLX W8SX42_ECOLX] Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.[HAMAP-Rule:MF_01541][PIRNR:PIRNR000207][SAAS:SAAS00040600]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Askenasy, I]]
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[[Category: Escherichia coli]]
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[[Category: Murray, D T]]
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[[Category: Large Structures]]
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[[Category: Pennington, J M]]
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[[Category: Askenasy I]]
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[[Category: Stroupe, M E]]
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[[Category: Murray DT]]
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[[Category: Tavolieri, A M]]
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[[Category: Pennington JM]]
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[[Category: Cytochrome p450 reductase]]
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[[Category: Stroupe ME]]
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[[Category: Electron transfer]]
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[[Category: Tavolieri AM]]
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[[Category: Fad]]
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[[Category: Flavoprotein]]
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[[Category: Fmn]]
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[[Category: Sulfite reductase]]
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[[Category: Sulfite reductase flavoprotein]]
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Current revision

The NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation that is unique to this diflavin reductase

PDB ID 6efv

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