3si2: Difference between revisions

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==Structure of glycosylated murine glutaminyl cyclase in presence of the inhibitor PQ50 (PDBD150)==
==Structure of glycosylated murine glutaminyl cyclase in presence of the inhibitor PQ50 (PDBD150)==
<StructureSection load='3si2' size='340' side='right' caption='[[3si2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3si2' size='340' side='right'caption='[[3si2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3si2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SI2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3si2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SI2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PBD:1-(3,4-DIMETHOXYPHENYL)-3-[3-(1H-IMIDAZOL-1-YL)PROPYL]THIOUREA'>PBD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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">[[3si1|3si1]], [[3si0|3si0]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PBD:1-(3,4-DIMETHOXYPHENYL)-3-[3-(1H-IMIDAZOL-1-YL)PROPYL]THIOUREA'>PBD</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene>, <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=10090 LK3 transgenic mice])</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=3si2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3si2 OCA], [https://pdbe.org/3si2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3si2 RCSB], [https://www.ebi.ac.uk/pdbsum/3si2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3si2 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=3si2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3si2 OCA], [http://pdbe.org/3si2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3si2 RCSB], [http://www.ebi.ac.uk/pdbsum/3si2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3si2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/QPCT_MOUSE QPCT_MOUSE] 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 (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glutaminyl-peptide cyclotransferase]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Carrillo, D]]
[[Category: Carrillo D]]
[[Category: Parthier, C]]
[[Category: Parthier C]]
[[Category: Stubbs, M T]]
[[Category: Stubbs MT]]
[[Category: Alpha/beta hydrolase]]
[[Category: Alzheimer's disease]]
[[Category: Glycoprotein]]
[[Category: Glycosylation]]
[[Category: Pe]]
[[Category: Pglu]]
[[Category: Pglu-amyloid]]
[[Category: Pyroglutamate]]
[[Category: Transferase-transferase inhibitor complex]]
Retrieved from "https://proteopedia.org/3si2"