4x1n: Difference between revisions

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 ==The crystal structure of mupain-1-16 in complex with murinised human uPA at pH7.4==
-<StructureSection load='4x1n' size='340' side='right' caption='[[4x1n]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='4x1n' size='340' side='right'caption='[[4x1n]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4x1n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X1N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X1N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4x1n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X1N FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MRZ:PIPERIDINE-1-CARBOXIMIDAMIDE'>MRZ</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]] 1.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x0w|4x0w]], [[4n1p|4n1p]], [[4n1q|4n1q]], [[4n1r|4n1r]], [[4n1s|4n1s]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MRZ:PIPERIDINE-1-CARBOXIMIDAMIDE'>MRZ</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/U-plasminogen_activator U-plasminogen activator], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.73 3.4.21.73] </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=4x1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x1n OCA], [https://pdbe.org/4x1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x1n RCSB], [https://www.ebi.ac.uk/pdbsum/4x1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x1n 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=4x1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x1n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x1n RCSB], [http://www.ebi.ac.uk/pdbsum/4x1n PDBsum]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/UROK_HUMAN UROK_HUMAN]] Defects in PLAU are the cause of Quebec platelet disorder (QPD) [MIM:[http://omim.org/entry/601709 601709]]. QPD is an autosomal dominant bleeding disorder due to a gain-of-function defect in fibrinolysis. Although affected individuals do not exhibit systemic fibrinolysis, they show delayed onset bleeding after challenge, such as surgery. The hallmark of the disorder is markedly increased PLAU levels within platelets, which causes intraplatelet plasmin generation and secondary degradation of alpha-granule proteins.<ref>PMID:20007542</ref>
+[https://www.uniprot.org/uniprot/UROK_HUMAN UROK_HUMAN] Defects in PLAU are the cause of Quebec platelet disorder (QPD) [MIM:[https://omim.org/entry/601709 601709]. QPD is an autosomal dominant bleeding disorder due to a gain-of-function defect in fibrinolysis. Although affected individuals do not exhibit systemic fibrinolysis, they show delayed onset bleeding after challenge, such as surgery. The hallmark of the disorder is markedly increased PLAU levels within platelets, which causes intraplatelet plasmin generation and secondary degradation of alpha-granule proteins.<ref>PMID:20007542</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/UROK_HUMAN UROK_HUMAN]] Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
+[https://www.uniprot.org/uniprot/UROK_HUMAN UROK_HUMAN] Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4x1n" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Plasminogen activator|Plasminogen activator]]
+*[[Urokinase 3D Structures|Urokinase 3D Structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: U-plasminogen activator]]
+[[Category: Homo sapiens]]
-[[Category: Andreasen, P]]
+[[Category: Large Structures]]
-[[Category: Huang, M]]
+[[Category: Synthetic construct]]
-[[Category: Jiang, L]]
+[[Category: Andreasen P]]
-[[Category: Xu, P]]
+[[Category: Huang M]]
-[[Category: Zhao, B]]
+[[Category: Jiang L]]
-[[Category: Hydrolase inhibitor-hydrolase complex]]
+[[Category: Xu P]]
-[[Category: Peptidic inhibitor]]
+[[Category: Zhao B]]
-[[Category: Serine protease]]
-[[Category: Upa]]