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Structure paper

TitleDevelopment and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureus.
Journal, issue, pagesProtein Sci., Vol. 23, Page 179-189, Year 2014
Publish dateOct 31, 2011 (structure data deposition date)
AuthorsBurchacka, E. / Zdzalik, M. / Niemczyk, J.S. / Pustelny, K. / Popowicz, G. / Wladyka, B. / Dubin, A. / Potempa, J. / Sienczyk, M. / Dubin, G. / Oleksyszyn, J.
External linksProtein Sci. / PubMed:24375505
MethodsX-ray diffraction
Resolution1.7 - 1.8 Å
Structure data

PDB-3ufa:
Crystal structure of the staphylococcal serine protease SplA in complex with a specific phosphonate inhibitor
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-4mvn:
Crystal structure of the staphylococcal serine protease SplA in complex with a specific phosphonate inhibitor
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-VPF:
N-(3-carboxypropanoyl)-L-valyl-N-[(1S)-2-phenyl-1-phosphonoethyl]-L-prolinamide

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-I1S:
[(1S)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl]phosphonic acid

Source
  • staphylococcus aureus (bacteria)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / chymotrypsin like fold / serine protease / extracellular protease / HYDROLASE-HYDROLASE INHIBITOR complex / CHYMOTRYPSIN-LIKE FOLD / SERINE ENDOPEPTIDASE / EXTRACELLULAR STAPHYLOCOCCAL PROTEASES

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