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3w8j

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Current revision (05:27, 3 August 2022) (edit) (undo)
 
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==Crystal structure of P5 a0 in a complex with Prx4 c-term==
==Crystal structure of P5 a0 in a complex with Prx4 c-term==
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<StructureSection load='3w8j' size='340' side='right' caption='[[3w8j]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='3w8j' size='340' side='right'caption='[[3w8j]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3w8j]] 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=3W8J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W8J FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3w8j]] is a 4 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=3W8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W8J FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vww|3vww]], [[3vwu|3vwu]], [[3vwv|3vwv]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vww|3vww]], [[3vwu|3vwu]], [[3vwv|3vwv]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDIA6, ERP5, P5, TXNDC7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDIA6, ERP5, P5, TXNDC7 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></td></tr>
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<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=3w8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w8j OCA], [http://pdbe.org/3w8j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3w8j RCSB], [http://www.ebi.ac.uk/pdbsum/3w8j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3w8j ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3w8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w8j OCA], [https://pdbe.org/3w8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w8j RCSB], [https://www.ebi.ac.uk/pdbsum/3w8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w8j ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PDIA6_HUMAN PDIA6_HUMAN]] May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.<ref>PMID:15466936</ref> <ref>PMID:12204115</ref> [[http://www.uniprot.org/uniprot/PRDX4_MOUSE PRDX4_MOUSE]] Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.
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[[https://www.uniprot.org/uniprot/PDIA6_HUMAN PDIA6_HUMAN]] May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.<ref>PMID:15466936</ref> <ref>PMID:12204115</ref> [[https://www.uniprot.org/uniprot/PRDX4_MOUSE PRDX4_MOUSE]] Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Protein disulfide-isomerase]]
[[Category: Protein disulfide-isomerase]]
[[Category: Inaba, K]]
[[Category: Inaba, K]]

Current revision

Crystal structure of P5 a0 in a complex with Prx4 c-term

PDB ID 3w8j

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