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2zyv
From Proteopedia
(Difference between revisions)
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==Crystal structure of mouse cytosolic sulfotransferase mSULT1D1 complex with PAPS/PAP and p-nitrophenol== | ==Crystal structure of mouse cytosolic sulfotransferase mSULT1D1 complex with PAPS/PAP and p-nitrophenol== | ||
| - | <StructureSection load='2zyv' size='340' side='right' caption='[[2zyv]], [[Resolution|resolution]] 1.81Å' scene=''> | + | <StructureSection load='2zyv' size='340' side='right'caption='[[2zyv]], [[Resolution|resolution]] 1.81Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2zyv]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2zyv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. The August 2009 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Sulfotransferases'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2009_8 10.2210/rcsb_pdb/mom_2009_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZYV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NPO:P-NITROPHENOL'>NPO</scene>, <scene name='pdbligand=PPS:3-PHOSPHATE-ADENOSINE-5-PHOSPHATE+SULFATE'>PPS</scene></td></tr> | + | </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=NPO:P-NITROPHENOL'>NPO</scene>, <scene name='pdbligand=PPS:3-PHOSPHATE-ADENOSINE-5-PHOSPHATE+SULFATE'>PPS</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zpt|2zpt]], [[2zvp|2zvp]], [[2zvq|2zvq]], [[2zyt|2zyt]], [[2zyu|2zyu]], [[2zyw|2zyw]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zpt|2zpt]], [[2zvp|2zvp]], [[2zvq|2zvq]], [[2zyt|2zyt]], [[2zyu|2zyu]], [[2zyw|2zyw]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sult1d1 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sult1d1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tyrosine-ester_sulfotransferase Tyrosine-ester sulfotransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.2.9 2.8.2.9] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zyv OCA], [https://pdbe.org/2zyv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zyv RCSB], [https://www.ebi.ac.uk/pdbsum/2zyv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zyv ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/ST1D1_MOUSE ST1D1_MOUSE]] Sulfotransferase with broad substrate specificity that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, such as dopamine, prostaglandins, leukotriene E4, drugs and xenobiotic compounds. Has sulfotransferase activity towards p-nitrophenol, 2-naphthylamine and minoxidil (in vitro). Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites.<ref>PMID:15087475</ref> <ref>PMID:18977225</ref> <ref>PMID:19966186</ref> <ref>PMID:9647753</ref> <ref>PMID:9920733</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Lk3 transgenic mice]] | [[Category: Lk3 transgenic mice]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
Revision as of 16:11, 22 December 2021
Crystal structure of mouse cytosolic sulfotransferase mSULT1D1 complex with PAPS/PAP and p-nitrophenol
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Categories: Large Structures | Lk3 transgenic mice | RCSB PDB Molecule of the Month | Sulfotransferases | Tyrosine-ester sulfotransferase | Kakuta, Y | Kimura, M | Liu, M C | Sakakibara, Y | Suiko, M | Teramoto, T | Michaelis complex | P-nitrophenol | Pap | Sulfonation mechanism | Sulfotransferase | Sult | Sult1d1 | Transferase

