This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6ash
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ==Crystal | + | ==Crystal structure of human Cathepsin K with a non-active site inhibitor at 1.42 Angstrom resolution== |
| - | <StructureSection load='6ash' size='340' side='right' caption='[[6ash]], [[Resolution|resolution]] 1.42Å' scene=''> | + | <StructureSection load='6ash' size='340' side='right'caption='[[6ash]], [[Resolution|resolution]] 1.42Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6ash]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ASH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ASH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ash]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ASH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ASH FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1XF:2-{[(CARBAMOYLSULFANYL)ACETYL]AMINO}BENZOIC+ACID'>1XF</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1XF:2-{[(CARBAMOYLSULFANYL)ACETYL]AMINO}BENZOIC+ACID'>1XF</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTSK, CTSO, CTSO2 ([http://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'>[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='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='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=6ash FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ash OCA], [http://pdbe.org/6ash PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ash RCSB], [http://www.ebi.ac.uk/pdbsum/6ash PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ash ProSAT]</span></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=6ash FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ash OCA], [http://pdbe.org/6ash PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ash RCSB], [http://www.ebi.ac.uk/pdbsum/6ash PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ash ProSAT]</span></td></tr> | ||
| Line 12: | Line 13: | ||
== 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. | [[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. | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Cathepsin 3D structures|Cathepsin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 17: | Line 21: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cathepsin K]] | [[Category: Cathepsin K]] | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Aguda, A]] | [[Category: Aguda, A]] | ||
[[Category: Brayer, G]] | [[Category: Brayer, G]] | ||
Revision as of 06:25, 21 August 2019
Crystal structure of human Cathepsin K with a non-active site inhibitor at 1.42 Angstrom resolution
| |||||||||||
