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TitlePhosphonate-based irreversible inhibitors of human gamma-glutamyl transpeptidase (GGT). GGsTop is a non-toxic and highly selective inhibitor with critical electrostatic interaction with an active-site residue Lys562 for enhanced inhibitory activity
Journal, issue, pagesBioorg. Med. Chem., Vol. 24, Page 5340-5352, Year 2016
Publish dateMay 18, 2016 (structure data deposition date)
AuthorsKamiyama, A. / Nakajima, M. / Han, L. / Wada, K. / Mizutani, M. / Tabuchi, Y. / Kojima-Yuasa, A. / Matsui-Yuasa, I. / Suzuki, H. / Fukuyama, K. ...Kamiyama, A. / Nakajima, M. / Han, L. / Wada, K. / Mizutani, M. / Tabuchi, Y. / Kojima-Yuasa, A. / Matsui-Yuasa, I. / Suzuki, H. / Fukuyama, K. / Watanabe, B. / Hiratake, J.
External linksBioorg. Med. Chem. / PubMed:27622749
MethodsX-ray diffraction
Resolution1.7 Å
Structure data

PDB-5b5t:
Crystal Structure of Escherichia coli Gamma-Glutamyltranspeptidase in Complex with peptidyl phosphonate inhibitor 1b
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-6FY:
(2~{S})-2-azanyl-4-[(2~{R})-1-(2-hydroxy-2-oxoethylamino)-1-oxidanylidene-butan-2-yl]oxyphosphonoyl-butanoic acid

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli (strain k12) (bacteria)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / glutathione / HYDROLASE-HYDROLASE INHIBITOR complex

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