3iej
From Proteopedia
(Difference between revisions)
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==Pyrazole-based Cathepsin S Inhibitors with Arylalkynes as P1 Binding Elements== | ==Pyrazole-based Cathepsin S Inhibitors with Arylalkynes as P1 Binding Elements== | ||
| - | <StructureSection load='3iej' size='340' side='right' caption='[[3iej]], [[Resolution|resolution]] 2.18Å' scene=''> | + | <StructureSection load='3iej' size='340' side='right'caption='[[3iej]], [[Resolution|resolution]] 2.18Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3iej]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3iej]] 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=3IEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IEJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=599:2-[3-{4-CHLORO-3-[(4-CHLOROPHENYL)ETHYNYL]PHENYL}-1-(3-MORPHOLIN-4-YLPROPYL)-1,4,6,7-TETRAHYDRO-5H-PYRAZOLO[4,3-C]PYRIDIN-5-YL]-2-OXOETHANOL'>599</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=599:2-[3-{4-CHLORO-3-[(4-CHLOROPHENYL)ETHYNYL]PHENYL}-1-(3-MORPHOLIN-4-YLPROPYL)-1,4,6,7-TETRAHYDRO-5H-PYRAZOLO[4,3-C]PYRIDIN-5-YL]-2-OXOETHANOL'>599</scene></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=3iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iej OCA], [https://pdbe.org/3iej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iej RCSB], [https://www.ebi.ac.uk/pdbsum/3iej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iej 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]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Cathepsin|Cathepsin]] | + | *[[Cathepsin 3D structures|Cathepsin 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Cathepsin S]] | [[Category: Cathepsin S]] | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Bembenek, S]] | [[Category: Bembenek, S]] | ||
[[Category: Cathepsin s]] | [[Category: Cathepsin s]] | ||
Revision as of 12:10, 13 October 2021
Pyrazole-based Cathepsin S Inhibitors with Arylalkynes as P1 Binding Elements
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Categories: Cathepsin S | Human | Large Structures | Bembenek, S | Cathepsin s | Disulfide bond | Glycoprotein | Hydrolase | Lysosome | Polymorphism | Protease | Thiol protease | Zymogen

