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<StructureSection load='1au0' size='340' side='right'caption='[[1au0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='1au0' size='340' side='right'caption='[[1au0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1au0]] is a 1 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=1AU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AU0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1au0]] is a 1 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=1AU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AU0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SDK:1,3-BIS[[N-[(PHENYLMETHOXY)CARBONYL]-L-LEUCYL]AMINO]-2-PROPANONE'>SDK</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]] 2.6&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cathepsin_K Cathepsin K], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.38 3.4.22.38] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SDK:1,3-BIS[[N-[(PHENYLMETHOXY)CARBONYL]-L-LEUCYL]AMINO]-2-PROPANONE'>SDK</scene></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=1au0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1au0 OCA], [https://pdbe.org/1au0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1au0 RCSB], [https://www.ebi.ac.uk/pdbsum/1au0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1au0 ProSAT]</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=1au0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1au0 OCA], [https://pdbe.org/1au0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1au0 RCSB], [https://www.ebi.ac.uk/pdbsum/1au0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1au0 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[https://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[https://omim.org/entry/265800 265800]]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref> <ref>PMID:9529353</ref> <ref>PMID:10491211</ref> <ref>PMID:10878663</ref>
[https://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[https://omim.org/entry/265800 265800]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref> <ref>PMID:9529353</ref> <ref>PMID:10491211</ref> <ref>PMID:10878663</ref>  
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.  
[https://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN] Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cathepsin K]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Abdel-Meguid, S S]]
[[Category: Abdel-Meguid SS]]
[[Category: Janson, C A]]
[[Category: Janson CA]]
[[Category: Smith, W W]]
[[Category: Smith WW]]
[[Category: Zhao, B]]
[[Category: Zhao B]]
[[Category: Hydrolase]]
[[Category: Sulfhydryl proteinase]]

Revision as of 10:56, 2 August 2023

CRYSTAL STRUCTURE OF THE CYSTEINE PROTEASE HUMAN CATHEPSIN K IN COMPLEX WITH A COVALENT SYMMETRIC DIACYLAMINOMETHYL KETONE INHIBITOR

1au0, resolution 2.60Å

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