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Structure paper

TitleCocrystal structures of primed side-extending alpha-ketoamide inhibitors reveal novel calpain-inhibitor aromatic interactions.
Journal, issue, pagesJ. Med. Chem., Vol. 51, Page 5264-5270, Year 2008
Publish dateSep 12, 2007 (structure data deposition date)
AuthorsQian, J. / Cuerrier, D. / Davies, P.L. / Li, Z. / Powers, J.C. / Campbell, R.L.
External linksJ. Med. Chem. / PubMed:18702462
MethodsX-ray diffraction
Resolution1.6 - 1.8 Å
Structure data

PDB-2r9c:
Calpain 1 proteolytic core inactivated by ZLAK-3001, an alpha-ketoamide
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2r9f:
Calpain 1 proteolytic core inactivated by ZLAK-3002, an alpha-ketoamide
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-GRD:
benzyl (S)-1-((2S,3S)-1-(3-(6-amino-9H-purin-9-yl)propylamino)-2-hydroxy-1-oxopentan-3-ylamino)-4-methyl-1-oxopentan-2-ylcarbamate

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-K2Z:
benzyl [(1S)-1-{[(1S,2S)-1-ethyl-2-hydroxy-3-{[3-(4-methylpiperazin-1-yl)propyl]amino}-3-oxopropyl]carbamoyl}-3-methylbutyl]carbamate

Source
  • rattus norvegicus (Norway rat)
KeywordsHYDROLASE / PROTEASE / PEPTIDASE / INHIBITOR / ALPHA-KETOAMIDE / Membrane / Thiol protease

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