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2r9o
From Proteopedia
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<StructureSection load='2r9o' size='340' side='right'caption='[[2r9o]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2r9o' size='340' side='right'caption='[[2r9o]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2r9o]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2r9o]] 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=2R9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R9O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=Y15:N-[(1S)-2-{[(1R)-2-(BENZYLOXY)-1-CYANO-1-METHYLETHYL]AMINO}-1-(CYCLOHEXYLMETHYL)-2-OXOETHYL]MORPHOLINE-4-CARBOXAMIDE'>Y15</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=Y15:N-[(1S)-2-{[(1R)-2-(BENZYLOXY)-1-CYANO-1-METHYLETHYL]AMINO}-1-(CYCLOHEXYLMETHYL)-2-OXOETHYL]MORPHOLINE-4-CARBOXAMIDE'>Y15</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2r9m|2r9m]], [[2r9n|2r9n]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2r9m|2r9m]], [[2r9n|2r9n]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTSS ([ | + | <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'>[ | + | <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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2r9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r9o OCA], [https://pdbe.org/2r9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r9o RCSB], [https://www.ebi.ac.uk/pdbsum/2r9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r9o ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == 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. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 04:19, 2 July 2021
Cathepsin S complexed with Compound 8
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Categories: Cathepsin S | Human | Large Structures | Bekkali, Y | Brown, M L | Capolino, A | Crane, K M | DeTuri, M | Emmanuel, M J | Freeman, D | Frye, L L | Girardot, M | Grygon, C A | Hao, M H | Hrapchak, M | Labadia, M E | Liu, W | Morwick, T | Nelson, R | Peterson, J D | Raymond, E L | Spero, D M | Thomson, D S | Wang, Y | Ward, Y D | White, A | White, D M | Wildeson, J | Young, E R.R | Zindell, R | Cathepsin | Glycoprotein | Hydrolase | Lysosome | Polymorphism | Protease | Thiol protease | Zymogen

