5qc7
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of human Cathepsin-S with bound ligand== | |
- | + | <StructureSection load='5qc7' size='340' side='right' caption='[[5qc7]], [[Resolution|resolution]] 1.90Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5qc7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5QC7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5QC7 FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BQS:2-[1-(cyclohexylmethyl)piperidin-4-yl]-1-{3-[3-{[2-(piperidin-1-yl)ethyl]sulfanyl}-4-(trifluoromethyl)phenyl]-1-propyl-1,4,6,7-tetrahydro-5H-pyrazolo[4,3-c]pyridin-5-yl}ethan-1-one'>BQS</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene></td></tr> | |
- | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </span></td></tr> |
- | [[Category: Burley, S]] | + | <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=5qc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5qc7 OCA], [http://pdbe.org/5qc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5qc7 RCSB], [http://www.ebi.ac.uk/pdbsum/5qc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5qc7 ProSAT]</span></td></tr> |
+ | </table> | ||
+ | == Function == | ||
+ | [[http://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. | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Cathepsin S]] | ||
+ | [[Category: Ameriks, M K]] | ||
+ | [[Category: Bembenek, S D]] | ||
+ | [[Category: Burley, S K]] | ||
+ | [[Category: Mirzadegan, T]] | ||
+ | [[Category: Shao, C]] | ||
[[Category: Yang, H]] | [[Category: Yang, H]] | ||
- | [[Category: | + | [[Category: Cathepsin s]] |
+ | [[Category: D3r]] | ||
+ | [[Category: Hydrolase]] | ||
+ | [[Category: Ligand docking]] |
Revision as of 06:14, 20 December 2017
Crystal structure of human Cathepsin-S with bound ligand
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Categories: Cathepsin S | Ameriks, M K | Bembenek, S D | Burley, S K | Mirzadegan, T | Shao, C | Yang, H | Cathepsin s | D3r | Hydrolase | Ligand docking