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3ctz

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{{STRUCTURE_3ctz| PDB=3ctz | SCENE= }}
 
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===Structure of human cytosolic X-prolyl aminopeptidase===
 
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{{ABSTRACT_PUBMED_18515364}}
 
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==Function==
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==Structure of human cytosolic X-prolyl aminopeptidase==
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[[http://www.uniprot.org/uniprot/XPP1_HUMAN XPP1_HUMAN]] Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro.
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<StructureSection load='3ctz' size='340' side='right'caption='[[3ctz]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[3ctz]] 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=3CTZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CTZ FirstGlance]. <br>
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[[3ctz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CTZ OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></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=3ctz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ctz OCA], [https://pdbe.org/3ctz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ctz RCSB], [https://www.ebi.ac.uk/pdbsum/3ctz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ctz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/XPP1_HUMAN XPP1_HUMAN] Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ct/3ctz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ctz ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Aminopeptidase|Aminopeptidase]]
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:018515364</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Xaa-Pro aminopeptidase]]
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[[Category: Large Structures]]
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[[Category: Li, X.]]
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[[Category: Li X]]
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[[Category: Lou, Z.]]
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[[Category: Lou Z]]
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[[Category: Rao, Z.]]
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[[Category: Rao Z]]
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[[Category: Aminopeptidase]]
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[[Category: Hydrolase]]
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[[Category: Manganese]]
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[[Category: Metal-binding]]
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[[Category: Metalloprotease]]
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[[Category: Pita-bread fold]]
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[[Category: Protease]]
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Current revision

Structure of human cytosolic X-prolyl aminopeptidase

PDB ID 3ctz

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