1ac5: Difference between revisions

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<StructureSection load='1ac5' size='340' side='right'caption='[[1ac5]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1ac5' size='340' side='right'caption='[[1ac5]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ac5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AC5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ac5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AC5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.4&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxypeptidase_D Carboxypeptidase D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.6 3.4.16.6] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=1ac5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ac5 OCA], [http://pdbe.org/1ac5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ac5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ac5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ac5 ProSAT]</span></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=1ac5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ac5 OCA], [https://pdbe.org/1ac5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ac5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ac5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ac5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KEX1_YEAST KEX1_YEAST]] Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from the precursors of K1, K2 and K28 killer toxins and a-factor (mating pheromone). Involved in the programmed cell death caused by defective N-glycosylation and contributes also to the active cell death program induced by acetic acid stress or during chronological aging. Promotes cell fusion by proteolytically processing substrates that act in parallel to PRM1 as an alternative fusion machine, as cell wall components, or both.<ref>PMID:3301004</ref> <ref>PMID:4364866</ref> <ref>PMID:773743</ref> <ref>PMID:3305079</ref> <ref>PMID:3301840</ref> <ref>PMID:1469044</ref> <ref>PMID:8416959</ref> <ref>PMID:10972812</ref> <ref>PMID:11988505</ref> <ref>PMID:17210951</ref> <ref>PMID:18474590</ref>
[https://www.uniprot.org/uniprot/KEX1_YEAST KEX1_YEAST] Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from the precursors of K1, K2 and K28 killer toxins and a-factor (mating pheromone). Involved in the programmed cell death caused by defective N-glycosylation and contributes also to the active cell death program induced by acetic acid stress or during chronological aging. Promotes cell fusion by proteolytically processing substrates that act in parallel to PRM1 as an alternative fusion machine, as cell wall components, or both.<ref>PMID:3301004</ref> <ref>PMID:4364866</ref> <ref>PMID:773743</ref> <ref>PMID:3305079</ref> <ref>PMID:3301840</ref> <ref>PMID:1469044</ref> <ref>PMID:8416959</ref> <ref>PMID:10972812</ref> <ref>PMID:11988505</ref> <ref>PMID:17210951</ref> <ref>PMID:18474590</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ac/1ac5_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ac/1ac5_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Carboxypeptidase D]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Cygler, M]]
[[Category: Cygler M]]
[[Category: Shilton, B H]]
[[Category: Shilton BH]]
[[Category: Thomas, D Y]]
[[Category: Thomas DY]]
[[Category: Carboxypeptidase]]
[[Category: Glycoprotein]]
[[Category: Hydrolase]]
[[Category: Transmembrane]]
Retrieved from "https://proteopedia.org/1ac5"