4r17

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==Ligand-induced aziridine-formation at subunit beta5 of the yeast 20S proteasome==
==Ligand-induced aziridine-formation at subunit beta5 of the yeast 20S proteasome==
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<StructureSection load='4r17' size='340' side='right' caption='[[4r17]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='4r17' size='340' side='right'caption='[[4r17]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4r17]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R17 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4r17]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R17 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=3K4:(2S,3S)-3-METHYLAZIRIDINE-2-CARBOXYLIC+ACID'>3K4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ryp|1ryp]], [[4r18|4r18]]</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=3K4:(2S,3S)-3-METHYLAZIRIDINE-2-CARBOXYLIC+ACID'>3K4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </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=4r17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r17 OCA], [https://pdbe.org/4r17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r17 RCSB], [https://www.ebi.ac.uk/pdbsum/4r17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r17 ProSAT]</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=4r17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r17 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r17 RCSB], [http://www.ebi.ac.uk/pdbsum/4r17 PDBsum]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PSA2_YEAST PSA2_YEAST] The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4r17" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Proteasome 3D structures|Proteasome 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Proteasome endopeptidase complex]]
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae s288c]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Brouwer, A J.]]
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[[Category: Brouwer AJ]]
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[[Category: Cui, H.]]
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[[Category: Cui H]]
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[[Category: Dubiella, C.]]
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[[Category: Dubiella C]]
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[[Category: Gersch, M.]]
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[[Category: Gersch M]]
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[[Category: Groll, M.]]
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[[Category: Groll M]]
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[[Category: Krueger, A.]]
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[[Category: Krueger A]]
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[[Category: Liskamp, R.]]
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[[Category: Liskamp R]]
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[[Category: Sieber, S A.]]
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[[Category: Sieber SA]]
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[[Category: Binding analysis]]
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[[Category: Crosslink]]
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[[Category: Drug development]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Proteasome]]
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[[Category: Umpolung]]
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Current revision

Ligand-induced aziridine-formation at subunit beta5 of the yeast 20S proteasome

PDB ID 4r17

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