4no6: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
m Protected "4no6" [edit=sysop:move=sysop]
No edit summary
 
(7 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 4no6 is ON HOLD
==yCP in complex with Z-Leu-Leu-Leu-vinylsulfone==
<StructureSection load='4no6' size='340' side='right'caption='[[4no6]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4no6]] 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=4NO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NO6 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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2M1:N-[(BENZYLOXY)CARBONYL]-L-LEUCYL-N-[(3S)-5-METHYL-1-(METHYLSULFONYL)HEXAN-3-YL]-L-LEUCINAMIDE'>2M1</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=4no6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4no6 OCA], [https://pdbe.org/4no6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4no6 RCSB], [https://www.ebi.ac.uk/pdbsum/4no6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4no6 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-vinylsulfone
__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]]

Latest revision as of 17:07, 13 March 2024

yCP in complex with Z-Leu-Leu-Leu-vinylsulfoneyCP in complex with Z-Leu-Leu-Leu-vinylsulfone

Structural highlights

4no6 is a 20 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

See Also

4no6, resolution 3.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA