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6hgy

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Current revision (05:17, 21 November 2024) (edit) (undo)
 
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<StructureSection load='6hgy' size='340' side='right'caption='[[6hgy]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='6hgy' size='340' side='right'caption='[[6hgy]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6hgy]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HGY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HGY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6hgy]] 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=6HGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HGY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G4B:THALASSOSPIRAMIDE+C'>G4B</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G4B:(~{Z})-~{N}-[(2~{S})-3-(4-hydroxyphenyl)-1-[[(2~{S})-1-[[(3~{S},6~{S},11~{R})-3-[(4-hydroxyphenyl)methyl]-2,5,8-tris(oxidanylidene)-6-propan-2-yl-1-oxa-4,7-diazacyclododec-11-yl]amino]-3-methyl-1-oxidanylidene-butan-2-yl]amino]-1-oxidanylidene-propan-2-yl]dec-3-enamide'>G4B</scene></td></tr>
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<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=6hgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hgy OCA], [http://pdbe.org/6hgy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hgy RCSB], [http://www.ebi.ac.uk/pdbsum/6hgy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hgy ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6hgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hgy OCA], [https://pdbe.org/6hgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hgy RCSB], [https://www.ebi.ac.uk/pdbsum/6hgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hgy ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[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>
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[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 ==
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[[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.
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[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 6hgy" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6hgy" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Cathepsin 3D structures|Cathepsin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cathepsin K]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Adler, M]]
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[[Category: Adler M]]
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[[Category: Blaesse, M]]
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[[Category: Blaesse M]]
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[[Category: Buckman, B O]]
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[[Category: Buckman BO]]
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[[Category: Griessner, A]]
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[[Category: Griessner A]]
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[[Category: Zakarian, A]]
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[[Category: Zakarian A]]
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[[Category: Cathepsin k]]
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[[Category: Hydrolase]]
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[[Category: Protease]]
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[[Category: Proteros biostructures gmbh]]
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Current revision

CRYSTAL STRUCTURE OF CATHEPSIN K WITH N-DESMETHYL THALASSOSPIRAMIDE C

PDB ID 6hgy

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