9vq5: Difference between revisions
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==Crystal structure of Peroxiredoxin I in complex with SAC== | |||
<StructureSection load='9vq5' size='340' side='right'caption='[[9vq5]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9vq5]] 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=9VQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VQ5 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]] 1.5Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1ES6:(2~{R})-3-[3,4-bis(oxidanyl)phenyl]-2-[(~{E})-3-[2-[3,4-bis(oxidanyl)phenyl]-7-oxidanyl-1-benzofuran-4-yl]prop-2-enoyl]oxy-propanoic+acid'>A1ES6</scene></td></tr> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9vq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vq5 OCA], [https://pdbe.org/9vq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vq5 RCSB], [https://www.ebi.ac.uk/pdbsum/9vq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vq5 ProSAT]</span></td></tr> | ||
[[Category: Luo | </table> | ||
[[Category: | == Function == | ||
[[Category: | [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). | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Luo C]] | |||
[[Category: Xu H]] | |||
[[Category: Zhang H]] | |||
[[Category: Zhu YY]] | |||
Latest revision as of 07:29, 8 July 2026
Crystal structure of Peroxiredoxin I in complex with SAC
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