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1glo

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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=1glo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1glo RCSB], [http://www.ebi.ac.uk/pdbsum/1glo PDBsum]</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=1glo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1glo RCSB], [http://www.ebi.ac.uk/pdbsum/1glo PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://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]]

Revision as of 23:41, 24 December 2014

CRYSTAL STRUCTURE OF CYS25SER MUTANT OF HUMAN CATHEPSIN S

1glo, resolution 2.20Å

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