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==Crystal Structure of the first catalytic domain of protein disulfide isomerase P5==
==Crystal Structure of the first catalytic domain of protein disulfide isomerase P5==
<StructureSection load='4ef0' size='340' side='right' caption='[[4ef0]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='4ef0' size='340' side='right'caption='[[4ef0]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ef0]] is a 2 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=4EF0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/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='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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<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>
<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>
<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=4ef0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ef0 OCA], [http://pdbe.org/4ef0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ef0 RCSB], [http://www.ebi.ac.uk/pdbsum/4ef0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ef0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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>
[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/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Protein disulfide-isomerase]]
[[Category: Large Structures]]
[[Category: Gehring, K]]
[[Category: Gehring K]]
[[Category: Kozlov, G]]
[[Category: Kozlov G]]
[[Category: Vinaik, R]]
[[Category: Vinaik R]]
[[Category: Bip]]
[[Category: Disulfide bond isomerization]]
[[Category: Endoplasmic reticulum]]
[[Category: Isomerase]]
[[Category: Thioredoxin-like fold]]

Latest revision as of 14:59, 14 March 2024

Crystal Structure of the first catalytic domain of protein disulfide isomerase P5

4ef0, resolution 1.50Å

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