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TitleAffinity Crystallography: A New Approach to Extracting High-Affinity Enzyme Inhibitors from Natural Extracts.
Journal, issue, pagesJ. Nat. Prod., Vol. 79, Page 1962-1970, Year 2016
Publish dateMar 19, 2015 (structure data deposition date)
AuthorsAguda, A.H. / Lavallee, V. / Cheng, P. / Bott, T.M. / Meimetis, L.G. / Law, S. / Nguyen, N.T. / Williams, D.E. / Kaleta, J. / Villanueva, I. ...Aguda, A.H. / Lavallee, V. / Cheng, P. / Bott, T.M. / Meimetis, L.G. / Law, S. / Nguyen, N.T. / Williams, D.E. / Kaleta, J. / Villanueva, I. / Davies, J. / Andersen, R.J. / Brayer, G.D. / Bromme, D.
External linksJ. Nat. Prod. / PubMed:27498895
MethodsX-ray diffraction
Resolution1.8 - 2 Å
Structure data

PDB-4yv8:
Crystal structure of cathepsin K bound to the covalent inhibitor lichostatinal
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-4yva:
Cathepsin K co-crystallized with actinomycetes extract
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • actinomycete 095-35 (bacteria)
KeywordsHYDROLASE/INHIBITOR / cathepsin K / lichostatinal / inhibitor / HYDROLASE-INHIBITOR complex / HYDROLASE / actinomycetes

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