4ef0: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ef0]] 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=4EF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EF0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ef0]] 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=4EF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EF0 FirstGlance]. <br> | ||
</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=4ef0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ef0 OCA], [https://pdbe.org/4ef0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ef0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ef0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ef0 ProSAT]</span></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]] 1.5Å</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=4ef0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ef0 OCA], [https://pdbe.org/4ef0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ef0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ef0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ef0 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[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> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 14:59, 14 March 2024
Crystal Structure of the first catalytic domain of protein disulfide isomerase P5
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