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5qca
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human Cathepsin-S with bound ligand== | |
| - | + | <StructureSection load='5qca' size='340' side='right' caption='[[5qca]], [[Resolution|resolution]] 2.29Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5qca]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5QCA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5QCA FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGJ:1-{4-[(2-chloro-5-{1-[3-(4-cyclopropylpiperazin-1-yl)propyl]-5-(methylsulfonyl)-4,5,6,7-tetrahydro-1H-pyrazolo[4,3-c]pyridin-3-yl}phenyl)ethynyl]phenyl}-N-[(4-chlorophenyl)methyl]methanamine'>BGJ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5qca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5qca OCA], [http://pdbe.org/5qca PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5qca RCSB], [http://www.ebi.ac.uk/pdbsum/5qca PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5qca 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
