5wqj
From Proteopedia
(Difference between revisions)
(One intermediate revision not shown.) | |||
Line 1: | Line 1: | ||
==Crystal structure of 3-Mercaptopyruvate Sulfurtransferase(3MST) in complex with compound1== | ==Crystal structure of 3-Mercaptopyruvate Sulfurtransferase(3MST) in complex with compound1== | ||
- | <StructureSection load='5wqj' size='340' side='right' caption='[[5wqj]], [[Resolution|resolution]] 1.20Å' scene=''> | + | <StructureSection load='5wqj' size='340' side='right'caption='[[5wqj]], [[Resolution|resolution]] 1.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[5wqj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WQJ OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5wqj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WQJ FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7N3:2-[2-[(4-oxidanylidene-3~{H}-quinazolin-2-yl)sulfanyl]ethanoylamino]thiophene-3-carboxamide'>7N3</scene>, <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=5wqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wqj OCA], [https://pdbe.org/5wqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wqj RCSB], [https://www.ebi.ac.uk/pdbsum/5wqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wqj ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/THTM_MOUSE THTM_MOUSE] Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H(2)S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions.<ref>PMID:18855522</ref> <ref>PMID:21937432</ref> <ref>PMID:22808324</ref> <ref>PMID:28079151</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Line 18: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5wqj" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5wqj" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Sulfurtransferase|Sulfurtransferase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Mus musculus]] |
- | [[Category: | + | [[Category: Shimizu T]] |
- | [[Category: | + | [[Category: Suwanai Y]] |
+ | [[Category: Toma-Fukai S]] |
Current revision
Crystal structure of 3-Mercaptopyruvate Sulfurtransferase(3MST) in complex with compound1
|