3ovx

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Revision as of 11:19, 21 February 2024

Cathepsin S in complex with a covalent inhibitor with an aldehyde warhead

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ovx"

Categories: Homo sapiens | Large Structures | Fradera X | Uitdehaag JCM | Van Zeeland M

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 <StructureSection load='3ovx' size='340' side='right'caption='[[3ovx]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ovx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OVX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ovx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OVX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=O64:2-CHLORO-N-[(1S)-1-FORMYLPROPYL]-3-(TRIFLUOROMETHYL)BENZAMIDE'>O64</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]] 1.49&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ovz|3ovz]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=O64:2-CHLORO-N-[(1S)-1-FORMYLPROPYL]-3-(TRIFLUOROMETHYL)BENZAMIDE'>O64</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTSS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </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=3ovx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ovx OCA], [https://pdbe.org/3ovx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ovx RCSB], [https://www.ebi.ac.uk/pdbsum/3ovx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ovx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CATS_HUMAN CATS_HUMAN]] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
+[https://www.uniprot.org/uniprot/CATS_HUMAN CATS_HUMAN] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The trifluoromethylphenyl P2 motif from previously reported heteroarylnitrile series has been successfully applied for the design and synthesis of highly potent novel ketoamide-based cathepsin S inhibitors. The key in this process is the change of the torsion angle between the P2 phenyl ring and the attached secondary amide by adding a small Cl, F, or Me group at the 2-position.
-Trifluoromethylphenyl as P2 for ketoamide-based cathepsin S inhibitors.,Cai J, Robinson J, Belshaw S, Everett K, Fradera X, van Zeeland M, van Berkom L, van Rijnsbergen P, Popplestone L, Baugh M, Dempster M, Bruin J, Hamilton W, Kinghorn E, Westwood P, Kerr J, Rankovic Z, Arbuckle W, Bennett DJ, Jones PS, Long C, Martin I, Uitdehaag JC, Meulemans T Bioorg Med Chem Lett. 2010 Dec 1;20(23):6890-4. Epub 2010 Oct 26. PMID:21030256<ref>PMID:21030256</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3ovx" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Cathepsin 3D structures|Cathepsin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Cathepsin S]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
 [[Category: Large Structures]]
-[[Category: Fradera, X]]
+[[Category: Fradera X]]
-[[Category: Uitdehaag, J C.M]]
+[[Category: Uitdehaag JCM]]
-[[Category: Zeeland, M van]]
+[[Category: Van Zeeland M]]
-[[Category: Aldehyde warhead]]
-[[Category: Cathepsin s]]
-[[Category: Covalent inhibitor]]
-[[Category: Hydrolase]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]
-[[Category: Ligand is covalently bound to cys25]]
-[[Category: Lysosomeal protein]]

3ovx

From Proteopedia

Revision as of 11:19, 21 February 2024

Cathepsin S in complex with a covalent inhibitor with an aldehyde warhead

Structural highlights

Function

See Also

Contents

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