3olh

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[[Image:3olh.png|left|200px]]
 
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{{STRUCTURE_3olh| PDB=3olh | SCENE= }}
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==Human 3-mercaptopyruvate sulfurtransferase==
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<StructureSection load='3olh' size='340' side='right'caption='[[3olh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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===Human 3-mercaptopyruvate sulfurtransferase===
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3olh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OLH FirstGlance]. <br>
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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]] 2.5&#8491;</td></tr>
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==About this Structure==
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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[[3olh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OLH OCA].
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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=3olh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3olh OCA], [https://pdbe.org/3olh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3olh RCSB], [https://www.ebi.ac.uk/pdbsum/3olh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3olh ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/THTM_HUMAN THTM_HUMAN] Encephalopathy due to beta-mercaptolactate-cysteine disulfiduria. Note=Aberrant MPST activity is found in a few cases of mercaptolactate-cysteine disulfiduria (MCDU) characterized by the appearance of large quantaties of the sulfur-containing amino acid, beta-mercaptolactate-cysteine disulfide, in the urine (PubMed:4973015, PubMed:4690911 and PubMed:6945862). Some cases have associated mental retardation (PubMed:4973015 and PubMed:6945862).
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== Function ==
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[https://www.uniprot.org/uniprot/THTM_HUMAN THTM_HUMAN] 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 (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ol/3olh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3olh ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
*[[Sulfurtransferase|Sulfurtransferase]]
*[[Sulfurtransferase|Sulfurtransferase]]
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[[Category: 3-mercaptopyruvate sulfurtransferase]]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Large Structures]]
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[[Category: Berg, S Van Den.]]
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[[Category: Arrowsmith CH]]
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[[Category: Berglund, H.]]
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[[Category: Berglund H]]
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[[Category: Bountra, C.]]
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[[Category: Bountra C]]
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[[Category: Collins, R.]]
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[[Category: Collins R]]
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[[Category: Edwards, A M.]]
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[[Category: Edwards AM]]
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[[Category: Flodin, S.]]
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[[Category: Flodin S]]
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[[Category: Flores, A.]]
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[[Category: Flores A]]
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[[Category: Graslund, S.]]
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[[Category: Graslund S]]
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[[Category: Hammarstrom, M.]]
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[[Category: Hammarstrom M]]
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[[Category: Johansson, I.]]
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[[Category: Johansson I]]
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[[Category: Karlberg, T.]]
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[[Category: Karlberg T]]
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[[Category: Kotenyova, T.]]
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[[Category: Kotenyova T]]
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[[Category: Kouznetsova, E.]]
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[[Category: Kouznetsova E]]
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[[Category: Moche, M.]]
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[[Category: Moche M]]
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[[Category: Nordlund, P.]]
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[[Category: Nordlund P]]
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[[Category: Nyman, T.]]
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[[Category: Nyman T]]
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[[Category: Persson, C.]]
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[[Category: Persson C]]
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[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: Schuler H]]
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[[Category: Schuler, H.]]
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[[Category: Schutz P]]
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[[Category: Schutz, P.]]
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[[Category: Sehic A]]
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[[Category: Sehic, A.]]
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[[Category: Siponen MI]]
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[[Category: Siponen, M I.]]
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[[Category: Thorsell AG]]
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[[Category: Thorsell, A G.]]
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[[Category: Tresaugues L]]
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[[Category: Tresaugues, L.]]
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[[Category: Van Den Berg S]]
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[[Category: Wahlberg, E.]]
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[[Category: Wahlberg E]]
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[[Category: Weigelt, J.]]
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[[Category: Weigelt J]]
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[[Category: Welin, M.]]
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[[Category: Welin M]]
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[[Category: Rhodanese fold]]
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[[Category: Sgc]]
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[[Category: Structural genomic]]
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[[Category: Structural genomics consortium]]
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[[Category: Transferase]]
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Current revision

Human 3-mercaptopyruvate sulfurtransferase

PDB ID 3olh

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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