4no8: Difference between revisions

New page: '''Unreleased structure''' The entry 4no8 is ON HOLD Authors: Stein, M.L., Cui, H., Beck, P., Dubiella, C., Voss, C., Krueger, A., Schmidt, B., Groll, M. Description: yCP in complex wi...
 
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'''Unreleased structure'''


The entry 4no8 is ON HOLD
==yCP in complex with Z-Leu-Leu-Leu-ketoamide==
<StructureSection load='4no8' size='340' side='right'caption='[[4no8]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4no8]] 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=4NO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NO8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2LV:N-[(BENZYLOXY)CARBONYL]-L-LEUCYL-N-[(2S,3S)-2-HYDROXY-5-METHYL-1-OXO-1-(PHENYLAMINO)HEXAN-3-YL]-L-LEUCINAMIDE'>2LV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4no8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4no8 OCA], [https://pdbe.org/4no8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4no8 RCSB], [https://www.ebi.ac.uk/pdbsum/4no8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4no8 ProSAT]</span></td></tr>
</table>
== Function ==
[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.


Authors: Stein, M.L., Cui, H., Beck, P., Dubiella, C., Voss, C., Krueger, A., Schmidt, B., Groll, M.
==See Also==
 
*[[Proteasome 3D structures|Proteasome 3D structures]]
Description: yCP in complex with Z-Leu-Leu-Leu-ketoamide
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Beck P]]
[[Category: Cui H]]
[[Category: Dubiella C]]
[[Category: Groll M]]
[[Category: Krueger A]]
[[Category: Schmidt B]]
[[Category: Stein ML]]
[[Category: Voss C]]

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