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TitleSemicarbazone-based inhibitors of cathepsin K, are they prodrugs for aldehyde inhibitors?
Journal, issue, pagesBioorg. Med. Chem. Lett., Vol. 16, Page 978-983, Year 2006
Publish dateAug 29, 2005 (structure data deposition date)
AuthorsAdkison, K.K. / Barrett, D.G. / Deaton, D.N. / Gampe, R.T. / Hassell, A.M. / Long, S.T. / McFadyen, R.B. / Miller, A.B. / Miller, L.R. / Payne, J.A. ...Adkison, K.K. / Barrett, D.G. / Deaton, D.N. / Gampe, R.T. / Hassell, A.M. / Long, S.T. / McFadyen, R.B. / Miller, A.B. / Miller, L.R. / Payne, J.A. / Shewchuk, L.M. / Wells-Knecht, K.J. / Willard, D.H. / Wright, L.L.
External linksBioorg. Med. Chem. Lett. / PubMed:16290936
MethodsX-ray diffraction
Resolution2.3 - 2.4 Å
Structure data

PDB-2aux:
Cathepsin K complexed with a semicarbazone inhibitor
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-2auz:
Cathepsin K complexed with a semicarbazone inhibitor
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-CT1:
(1R)-2-METHYL-1-(PHENYLMETHYL)PROPYL[(1S)-1-FORMYLPENTYL]CARBAMATE

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-CT2:
1-(PHENYLMETHYL)CYCLOPENTYL[(1S)-1-FORMYLPENTYL]CARBAMATE

Source
  • homo sapiens (human)
KeywordsHYDROLASE / catK / cysteine protease

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