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2zen

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==Crystal structure of the human glutaminyl cyclase mutant D305A at 1.78 angstrom resolution==
==Crystal structure of the human glutaminyl cyclase mutant D305A at 1.78 angstrom resolution==
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<StructureSection load='2zen' size='340' side='right' caption='[[2zen]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
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<StructureSection load='2zen' size='340' side='right'caption='[[2zen]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2zen]] 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=2ZEN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZEN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2zen]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZEN FirstGlance]. <br>
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</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>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2afm|2afm]], [[2zed|2zed]], [[2zee|2zee]], [[2zef|2zef]], [[2zeg|2zeg]], [[2zeh|2zeh]], [[2zel|2zel]], [[2zem|2zem]], [[2zeo|2zeo]], [[2zep|2zep]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2afm|2afm]], [[2zed|2zed]], [[2zee|2zee]], [[2zef|2zef]], [[2zeg|2zeg]], [[2zeh|2zeh]], [[2zel|2zel]], [[2zem|2zem]], [[2zeo|2zeo]], [[2zep|2zep]]</div></td></tr>
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<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 HUMAN])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">QPCT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></td></tr>
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<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=2zen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zen OCA], [http://pdbe.org/2zen PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zen RCSB], [http://www.ebi.ac.uk/pdbsum/2zen PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zen ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zen OCA], [https://pdbe.org/2zen PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zen RCSB], [https://www.ebi.ac.uk/pdbsum/2zen PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zen ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Glutaminyl-peptide cyclotransferase]]
[[Category: Glutaminyl-peptide cyclotransferase]]
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Chang, E C]]
[[Category: Chang, E C]]
[[Category: Chou, T L]]
[[Category: Chou, T L]]

Revision as of 07:15, 10 November 2021

Crystal structure of the human glutaminyl cyclase mutant D305A at 1.78 angstrom resolution

PDB ID 2zen

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