3hy2: Difference between revisions

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 ==Crystal Structure of Sulfiredoxin in Complex with Peroxiredoxin I and ATP:Mg2+==
-<StructureSection load='3hy2' size='340' side='right' caption='[[3hy2]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='3hy2' size='340' side='right'caption='[[3hy2]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3hy2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HY2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HY2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3hy2]] is a 4 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=3HY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HY2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xw4|1xw4]], [[1xw3|1xw3]], [[3cyi|3cyi]], [[2rii|2rii]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRDX1, PAGA, PAGB, TDPX2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), C20orf139, SRX, SRXN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3hy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hy2 OCA], [https://pdbe.org/3hy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hy2 RCSB], [https://www.ebi.ac.uk/pdbsum/3hy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hy2 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peroxiredoxin Peroxiredoxin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.15 1.11.1.15] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hy2 OCA], [http://pdbe.org/3hy2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hy2 RCSB], [http://www.ebi.ac.uk/pdbsum/3hy2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hy2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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). [[http://www.uniprot.org/uniprot/SRXN1_HUMAN SRXN1_HUMAN]] Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase.<ref>PMID:15448164</ref> <ref>PMID:15590625</ref>
+[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).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hy/3hy2_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
@@ Line 33: / Line 31: @@
 ==See Also==
-*[[Peroxiredoxin|Peroxiredoxin]]
+*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Peroxiredoxin]]
+[[Category: Large Structures]]
-[[Category: Johnson, L C]]
+[[Category: Johnson LC]]
-[[Category: Jonsson, T J]]
+[[Category: Jonsson TJ]]
-[[Category: Lowther, W T]]
+[[Category: Lowther WT]]
-[[Category: Antioxidant]]
-[[Category: Atp-binding]]
-[[Category: Disulfide bond]]
-[[Category: Magnesium]]
-[[Category: Nucleotide-binding]]
-[[Category: Oxidoreductase]]
-[[Category: Peroxidase]]
-[[Category: Phosphoprotein]]
-[[Category: Protein repair]]
-[[Category: Protein-protein complex]]
-[[Category: Redox biology]]
-[[Category: Redox-active center]]
-[[Category: Sulfur chemistry]]