4dgj
From Proteopedia
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==Structure of a human enteropeptidase light chain variant== | ==Structure of a human enteropeptidase light chain variant== | ||
- | <StructureSection load='4dgj' size='340' side='right' caption='[[4dgj]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='4dgj' size='340' side='right'caption='[[4dgj]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4dgj]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4dgj]] 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=4DGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DGJ FirstGlance]. <br> |
- | </td></tr><tr><td class="sblockLbl"><b>[[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=4dgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dgj OCA], [https://pdbe.org/4dgj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dgj RCSB], [https://www.ebi.ac.uk/pdbsum/4dgj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dgj ProSAT]</span></td></tr> | |
- | <tr | + | </table> |
- | + | ||
- | <table> | + | |
== Disease == | == Disease == | ||
- | [ | + | [https://www.uniprot.org/uniprot/ENTK_HUMAN ENTK_HUMAN] Congenital enteropathy due to enteropeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry. |
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/ENTK_HUMAN ENTK_HUMAN] Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
+ | <div class="pdbe-citations 4dgj" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Enteropeptidase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Simeonov P]] |
- | [[Category: | + | [[Category: Straeter N]] |
- | [[Category: | + | [[Category: Zahn M]] |
- | + |
Current revision
Structure of a human enteropeptidase light chain variant
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