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3h8q
From Proteopedia
(Difference between revisions)
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==Crystal structure of glutaredoxin domain of human thioredoxin reductase 3== | ==Crystal structure of glutaredoxin domain of human thioredoxin reductase 3== | ||
| - | <StructureSection load='3h8q' size='340' side='right' caption='[[3h8q]], [[Resolution|resolution]] 2.21Å' scene=''> | + | <StructureSection load='3h8q' size='340' side='right'caption='[[3h8q]], [[Resolution|resolution]] 2.21Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3h8q]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3h8q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGR, TRXR3, TXNRD3, TXNRD3 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGR, TRXR3, TXNRD3, TXNRD3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </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=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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Thioredoxin | + | *[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]] |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Thioredoxin-disulfide reductase]] | [[Category: Thioredoxin-disulfide reductase]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
Revision as of 08:06, 16 March 2022
Crystal structure of glutaredoxin domain of human thioredoxin reductase 3
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Categories: Human | Large Structures | Thioredoxin-disulfide reductase | Arrowsmith, C H | Bountra, C | Chaikuad, A | Delft, F von | Edwards, A M | Johansson, C | Oppermann, U | Pilka, E | Roos, A K | Structural genomic | Ugochukwu, E | Weigelt, J | Yue, W | Developmental protein | Differentiation | Disulfide bond | Electron transport | Endoplasmic reticulum | Fad | Flavoprotein | Microsome | Nadp | Nucleus | Oxidoreductase | Phosphoprotein | Redox-active center | Selenium | Selenocysteine | Sgc | Spermatogenesis | Transport
