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6p5x

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Current revision (07:23, 11 October 2023) (edit) (undo)
 
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<StructureSection load='6p5x' size='340' side='right'caption='[[6p5x]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
<StructureSection load='6p5x' size='340' side='right'caption='[[6p5x]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6p5x]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P5X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P5X FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6p5x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P5X 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SHN:3,3,3,3-[(7S,8S,12S,13S)-3,8,13,17-tetrakis(carboxymethyl)-8,13-dimethyl-7,8,12,13-tetrahydroporphyrin-2,7,12,18-tetrayl]tetrapropanoic+acid'>SHN</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]] 1.97&#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/Uroporphyrinogen-III_C-methyltransferase Uroporphyrinogen-III C-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.107 2.1.1.107] </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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SHN:3,3,3,3-[(7S,8S,12S,13S)-3,8,13,17-tetrakis(carboxymethyl)-8,13-dimethyl-7,8,12,13-tetrahydroporphyrin-2,7,12,18-tetrayl]tetrapropanoic+acid'>SHN</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=6p5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p5x OCA], [http://pdbe.org/6p5x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p5x RCSB], [http://www.ebi.ac.uk/pdbsum/6p5x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p5x 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=6p5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p5x OCA], [https://pdbe.org/6p5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p5x RCSB], [https://www.ebi.ac.uk/pdbsum/6p5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p5x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/A0A0F7JCI1_SALER A0A0F7JCI1_SALER]] Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.[HAMAP-Rule:MF_01646][SAAS:SAAS00971394]
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[https://www.uniprot.org/uniprot/CYSG_SALTY CYSG_SALTY] Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.<ref>PMID:14595395</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6p5x" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6p5x" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Siroheme synthase|Siroheme synthase]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Uroporphyrinogen-III C-methyltransferase]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Pennington, J M]]
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[[Category: Pennington JM]]
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[[Category: Stroupe, M E]]
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[[Category: Stroupe ME]]
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[[Category: Biosynthetic protein]]
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[[Category: Cysg]]
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[[Category: Precorrin-2]]
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[[Category: Sirohydrochlorin]]
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[[Category: Tetrapyrrole biosynthesis]]
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Current revision

Sirohydrochlorin-bound S. typhimurium siroheme synthase

PDB ID 6p5x

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