3pb4: Difference between revisions

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==Crystal structure of the catalytic domain of human Golgi-resident glutaminyl cyclase at pH 6.0==
The line below this paragraph, containing "STRUCTURE_3pb4", creates the "Structure Box" on the page.
<StructureSection load='3pb4' size='340' side='right'caption='[[3pb4]], [[Resolution|resolution]] 1.13&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3pb4]] is a 1 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=3PB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PB4 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.13&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_3pb4|  PDB=3pb4  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pb4 OCA], [https://pdbe.org/3pb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pb4 RCSB], [https://www.ebi.ac.uk/pdbsum/3pb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pb4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/QPCTL_HUMAN QPCTL_HUMAN] Responsible for the biosynthesis of pyroglutamyl peptides.<ref>PMID:18486145</ref> <ref>PMID:21288892</ref>


===Crystal structure of the catalytic domain of human Golgi-resident glutaminyl cyclase at pH 6.0===
==See Also==
 
*[[Glutaminyl cyclase|Glutaminyl cyclase]]
 
== References ==
==About this Structure==
<references/>
[[3pb4]] is a 1 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=3PB4 OCA].
__TOC__
[[Category: Glutaminyl-peptide cyclotransferase]]
</StructureSection>
[[Category: Homo sapiens]]
[[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: Wang AHJ]]

Latest revision as of 16:30, 1 March 2024

Crystal structure of the catalytic domain of human Golgi-resident glutaminyl cyclase at pH 6.0Crystal structure of the catalytic domain of human Golgi-resident glutaminyl cyclase at pH 6.0

Structural highlights

3pb4 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.13Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

QPCTL_HUMAN Responsible for the biosynthesis of pyroglutamyl peptides.[1] [2]

See Also

References

  1. ↑ Cynis H, Rahfeld JU, Stephan A, Kehlen A, Koch B, Wermann M, Demuth HU, Schilling S. Isolation of an isoenzyme of human glutaminyl cyclase: retention in the Golgi complex suggests involvement in the protein maturation machinery. J Mol Biol. 2008 Jun 20;379(5):966-80. doi: 10.1016/j.jmb.2008.03.078. Epub 2008 , Apr 15. PMID:18486145 doi:http://dx.doi.org/10.1016/j.jmb.2008.03.078
  2. ↑ Huang KF, Liaw SS, Huang WL, Chia CY, Lo YC, Chen YL, Wang AH. Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding. J Biol Chem. 2011 Apr 8;286(14):12439-49. Epub 2011 Feb 1. PMID:21288892 doi:10.1074/jbc.M110.208595

3pb4, resolution 1.13Å

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