3pbe: Difference between revisions

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 ==Crystal structure of the mutant W207F of human secretory glutaminyl cyclase==
-<StructureSection load='3pbe' size='340' side='right' caption='[[3pbe]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+<StructureSection load='3pbe' size='340' side='right'caption='[[3pbe]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3pbe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PBE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3pbe]] 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=3PBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PBE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.95&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2afm|2afm]], [[3pb4|3pb4]], [[3pb6|3pb6]], [[3pb7|3pb7]], [[3pb8|3pb8]], [[3pb9|3pb9]], [[3pbb|3pbb]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">QPCT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3pbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pbe OCA], [https://pdbe.org/3pbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pbe RCSB], [https://www.ebi.ac.uk/pdbsum/3pbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pbe ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </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=3pbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pbe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pbe RCSB], [http://www.ebi.ac.uk/pdbsum/3pbe PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN]] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>
+[https://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3pbe" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 26: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Glutaminyl-peptide cyclotransferase]]
 [[Category: Homo sapiens]]
-[[Category: Chen, Y L]]
+[[Category: Large Structures]]
-[[Category: Chia, C Y]]
+[[Category: Chen YL]]
-[[Category: Huang, K F]]
+[[Category: Chia CY]]
-[[Category: Huang, W L]]
+[[Category: Huang KF]]
-[[Category: Liaw, S S]]
+[[Category: Huang WL]]
-[[Category: Lo, Y C]]
+[[Category: Liaw SS]]
-[[Category: Wang, A H.J]]
+[[Category: Lo YC]]
-[[Category: Alpha/beta protein]]
+[[Category: Wang AHJ]]
-[[Category: Alpha/beta-mixed fold]]
-[[Category: Glutaminyl cyclase]]
-[[Category: Secretory pathway]]
-[[Category: Transferase]]