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==Human cathepsin K mutant C25S==
==Human cathepsin K mutant C25S==
<StructureSection load='5jh3' size='340' side='right' caption='[[5jh3]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='5jh3' size='340' side='right'caption='[[5jh3]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5jh3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JH3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JH3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5jh3]] 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=5JH3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JH3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.75&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_K Cathepsin K], with EC number [http://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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<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=5jh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jh3 OCA], [http://pdbe.org/5jh3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jh3 RCSB], [http://www.ebi.ac.uk/pdbsum/5jh3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jh3 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=5jh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jh3 OCA], [https://pdbe.org/5jh3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jh3 RCSB], [https://www.ebi.ac.uk/pdbsum/5jh3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jh3 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[http://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 ==
[[http://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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5jh3" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5jh3" style="background-color:#fffaf0;"></div>
==See Also==
*[[Cathepsin 3D structures|Cathepsin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cathepsin K]]
[[Category: Homo sapiens]]
[[Category: Korenc, M]]
[[Category: Large Structures]]
[[Category: Lenarcic, B]]
[[Category: Korenc M]]
[[Category: Novinec, M]]
[[Category: Lenarcic B]]
[[Category: Allostery cysteine]]
[[Category: Novinec M]]
[[Category: Collagenase]]
[[Category: Enzyme regulation]]
[[Category: Hydrolase]]
[[Category: Peptidase proteolysis]]

Latest revision as of 18:51, 20 September 2023

Human cathepsin K mutant C25S

5jh3, resolution 1.75Å

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