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3h8q
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3h8q is ON HOLD Authors: Chaikuad, A., Johansson, C., Ugochukwu, E., Roos, A.K., von Delft, F., Pilka, E., Yue, W., Arrowsmith, C.H., Edwards, A.M.,...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of glutaredoxin domain of human thioredoxin reductase 3== | |
| + | <StructureSection load='3h8q' size='340' side='right'caption='[[3h8q]], [[Resolution|resolution]] 2.21Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3h8q]] is a 2 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=3H8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H8Q FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21Å</td></tr> | ||
| + | <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=SO4:SULFATE+ION'>SO4</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=3h8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8q OCA], [https://pdbe.org/3h8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h8q RCSB], [https://www.ebi.ac.uk/pdbsum/3h8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h8q ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TRXR3_HUMAN TRXR3_HUMAN] Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. Catalyzes disulfide bond isomerization. Promotes disulfide bond formation between GPX4 and various sperm proteins and may play a role in sperm maturation by promoting formation of sperm structural components (By similarity).[UniProtKB:Q99MD6] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h8/3h8q_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3h8q ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Homo sapiens]] | |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arrowsmith CH]] | ||
| + | [[Category: Bountra C]] | ||
| + | [[Category: Chaikuad A]] | ||
| + | [[Category: Edwards AM]] | ||
| + | [[Category: Johansson C]] | ||
| + | [[Category: Oppermann U]] | ||
| + | [[Category: Pilka E]] | ||
| + | [[Category: Roos AK]] | ||
| + | [[Category: Ugochukwu E]] | ||
| + | [[Category: Weigelt J]] | ||
| + | [[Category: Yue W]] | ||
| + | [[Category: Von Delft F]] | ||
Current revision
Crystal structure of glutaredoxin domain of human thioredoxin reductase 3
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Categories: Homo sapiens | Large Structures | Arrowsmith CH | Bountra C | Chaikuad A | Edwards AM | Johansson C | Oppermann U | Pilka E | Roos AK | Ugochukwu E | Weigelt J | Yue W | Von Delft F
