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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of cysteine protease human cathepsin k in complex with a covalent peptidomimetic inhibitor
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Structure:
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Cathepsin k. Chain: a. Engineered: yes. Other_details: inhibitor covalently bound to active site cys 25
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Cell_line: sf21. Cell: osteoclast. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf21.
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Resolution:
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2.30Å
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R-factor:
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0.240
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R-free:
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0.296
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Authors:
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R.L.Desjarlais,D.S.Yamashita,H.-J.Oh,W.E.Bondinell, I.N.Uzinskas,K.F.Erhard,A.C.Allen,R.C.Haltiwanger,B.Zhao, W.W.Smith,S.S.Abdel-Meguid,K.D'Alessio,C.A.Janson, M.S.Mcqueney,T.A.Tomaszek,M.A.Levy,D.F.Veber
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Key ref:
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R.L.Desjarlais
et al.
(1998).
Use of X-Ray co-Crystal structures and molecular modeling to design potent and selective non-Peptide inhibitors of cathepsin k.
J am chem soc,
120,
PubMed id:
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Date:
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29-May-98
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Release date:
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08-Jun-99
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PROCHECK
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Headers
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References
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P43235
(CATK_HUMAN) -
Cathepsin K
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Seq:
Struc:
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329 a.a.
215 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.3.4.22.38
- Cathepsin K.
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Reaction:
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Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg.
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Gene Ontology (GO) functional annotation
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Biological process
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proteolysis
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1 term
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Biochemical function
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cysteine-type peptidase activity
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2 terms
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Links
