4xcs
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Human peroxiredoxin-1 C83S mutant== | |
| + | <StructureSection load='4xcs' size='340' side='right'caption='[[4xcs]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4xcs]] is a 6 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=4XCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XCS 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]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4xcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xcs OCA], [https://pdbe.org/4xcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xcs RCSB], [https://www.ebi.ac.uk/pdbsum/4xcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xcs ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PRDX1_HUMAN PRDX1_HUMAN] Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity). | ||
| - | + | ==See Also== | |
| - | + | *[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]] | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Chang | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Chang T-S]] |
| - | [[Category: | + | [[Category: Cho A]] |
| - | [[Category: | + | [[Category: Cho KJ]] |
| - | [[Category: | + | [[Category: Khan TG]] |
| - | [[Category: | + | [[Category: Kim KH]] |
| + | [[Category: Lee J-H]] | ||
| + | [[Category: Park Y]] | ||
Current revision
Human peroxiredoxin-1 C83S mutant
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Categories: Homo sapiens | Large Structures | Chang T-S | Cho A | Cho KJ | Khan TG | Kim KH | Lee J-H | Park Y
