5B5T
Crystal Structure of Escherichia coli Gamma-Glutamyltranspeptidase in Complex with peptidyl phosphonate inhibitor 1b
Summary for 5B5T
Entry DOI | 10.2210/pdb5b5t/pdb |
Descriptor | Gamma-glutamyltranspeptidase large chain, Gamma-glutamyltranspeptidase small chain, (2~{S})-2-azanyl-4-[(2~{R})-1-(2-hydroxy-2-oxoethylamino)-1-oxidanylidene-butan-2-yl]oxyphosphonoyl-butanoic acid, ... (5 entities in total) |
Functional Keywords | glutathione, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Escherichia coli (strain K12) More |
Total number of polymer chains | 4 |
Total formula weight | 119380.05 |
Authors | Wada, K.,Fukuyama, K. (deposition date: 2016-05-18, release date: 2016-09-28, Last modification date: 2023-11-08) |
Primary citation | 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. Phosphonate-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 Bioorg.Med.Chem., 24:5340-5352, 2016 Cited by PubMed: 27622749DOI: 10.1016/j.bmc.2016.08.050 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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