3okj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:41, 6 September 2023) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Alpha-keto-aldehyde binding mechanism reveals a novel lead structure motif for proteasome inhibition==
==Alpha-keto-aldehyde binding mechanism reveals a novel lead structure motif for proteasome inhibition==
-
<StructureSection load='3okj' size='340' side='right' caption='[[3okj]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+
<StructureSection load='3okj' size='340' side='right'caption='[[3okj]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3okj]] is a 28 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=3OKJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OKJ FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3okj]] is a 20 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=3OKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OKJ FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EP9:N-[(BENZYLOXY)CARBONYL]-L-LEUCYL-N-[(2S,3S)-3-HYDROXY-1-(4-HYDROXYPHENYL)-4-OXOBUTAN-2-YL]-L-LEUCINAMIDE'>EP9</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]] 2.7&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ryp|1ryp]], [[1j2q|1j2q]], [[3d29|3d29]], [[1g65|1g65]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EP9:N-[(BENZYLOXY)CARBONYL]-L-LEUCYL-N-[(2S,3S)-3-HYDROXY-1-(4-HYDROXYPHENYL)-4-OXOBUTAN-2-YL]-L-LEUCINAMIDE'>EP9</scene></td></tr>
-
<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>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3okj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3okj OCA], [https://pdbe.org/3okj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3okj RCSB], [https://www.ebi.ac.uk/pdbsum/3okj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3okj ProSAT]</span></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=3okj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3okj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3okj RCSB], [http://www.ebi.ac.uk/pdbsum/3okj PDBsum]</span></td></tr>
+
</table>
</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.
==See Also==
==See Also==
-
*[[Proteasome|Proteasome]]
+
*[[Proteasome 3D structures|Proteasome 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Proteasome endopeptidase complex]]
+
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Gallastegui, P]]
+
[[Category: Gallastegui P]]
-
[[Category: Groll, M]]
+
[[Category: Groll M]]
-
[[Category: Huber, R]]
+
[[Category: Huber R]]
-
[[Category: Kloetzel, PM]]
+
[[Category: Kloetzel PM]]
-
[[Category: Poynor, M]]
+
[[Category: Poynor M]]
-
[[Category: Schmidt, B]]
+
[[Category: Schmidt B]]
-
[[Category: Stein, M]]
+
[[Category: Stein M]]
-
[[Category: Central antiparallel beta-sheet flanked by helice]]
+
-
[[Category: Cytosol]]
+
-
[[Category: Hydrolase-hydrolase inhibitor complex]]
+
-
[[Category: Inhibitor]]
+
-
[[Category: Nucleus]]
+
-
[[Category: Protease]]
+
-
[[Category: Turnover of ubiquitinated substrate]]
+
-
[[Category: Ubiquitin]]
+

Current revision

Alpha-keto-aldehyde binding mechanism reveals a novel lead structure motif for proteasome inhibition

PDB ID 3okj

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools