4fzc

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==20S yeast proteasome in complex with cepafungin I==
==20S yeast proteasome in complex with cepafungin I==
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<StructureSection load='4fzc' size='340' side='right' caption='[[4fzc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='4fzc' size='340' side='right'caption='[[4fzc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fzc]] is a 32 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=4FZC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FZC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fzc]] 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=4FZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FZC FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0W5:(2E,4E)-11-METHYLDODECA-2,4-DIENOIC+ACID'>0W5</scene>, <scene name='pdbligand=0W6:(4S)-4-AMINOPENTANOIC+ACID'>0W6</scene>, <scene name='pdbligand=LYO:4-HYDROXY-LYSINE'>LYO</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]] 2.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ryp|1ryp]], [[2zcy|2zcy]]</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=0W5:(2E,4E)-11-METHYLDODECA-2,4-DIENOIC+ACID'>0W5</scene>, <scene name='pdbligand=0W6:(4S)-4-AMINOPENTANOIC+ACID'>0W6</scene>, <scene name='pdbligand=LYO:4-HYDROXY-LYSINE'>LYO</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=4fzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fzc OCA], [https://pdbe.org/4fzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fzc RCSB], [https://www.ebi.ac.uk/pdbsum/4fzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fzc 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=4fzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fzc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fzc RCSB], [http://www.ebi.ac.uk/pdbsum/4fzc 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 4fzc" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Proteasome|Proteasome]]
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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]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Beck, P]]
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[[Category: Beck P]]
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[[Category: Becker, C F.W]]
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[[Category: Becker CFW]]
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[[Category: Dudler, R]]
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[[Category: Dudler R]]
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[[Category: Groll, M]]
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[[Category: Groll M]]
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[[Category: Kaiser, M]]
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[[Category: Kaiser M]]
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[[Category: Stein, M]]
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[[Category: Stein M]]
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[[Category: Drug development]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Inhibitor]]
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[[Category: N-terminal nucleophilic hydrolase]]
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[[Category: Natural product]]
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[[Category: Proteasome]]
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[[Category: Protein degradation]]
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[[Category: Ubiquitin]]
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Current revision

20S yeast proteasome in complex with cepafungin I

PDB ID 4fzc

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