5BPK
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![BU of 5bpk by Molmil](/molmil-images/mine/5bpk) | Varying binding modes of inhibitors and structural differences in the binding pockets of different gamma-glutamyltranspeptidases | Descriptor: | (2S)-amino[(5S)-4,5-dihydro-1,2-oxazol-5-yl]acetic acid, 1,2-ETHANEDIOL, Gamma-glutamyltranspeptidase (Ggt) | Authors: | Bolz, C, Bach, N.C, Meyer, H, Mueller, G, Dawidowski, M, Popowicz, G, Sieber, S.A, Skerra, A, Gerhard, M. | Deposit date: | 2015-05-28 | Release date: | 2016-05-18 | Last modified: | 2024-01-10 | Method: | X-RAY DIFFRACTION (1.49 Å) | Cite: | Varying binding modes of inhibitors and structural differences in the binding pockets of different gamma-glutamyltranspeptidases To Be Published
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2QMC
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![BU of 2qmc by Molmil](/molmil-images/mine/2qmc) | |
2QM6
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![BU of 2qm6 by Molmil](/molmil-images/mine/2qm6) | |
3FNM
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![BU of 3fnm by Molmil](/molmil-images/mine/3fnm) | Crystal structure of acivicin-inhibited gamma-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis | Descriptor: | (2S)-AMINO[(5S)-3-CHLORO-4,5-DIHYDROISOXAZOL-5-YL]ACETIC ACID, Gamma-glutamyltranspeptidase (Ggt) Large subunit, Gamma-glutamyltranspeptidase (Ggt) Small subunit | Authors: | Williams, K, Cullati, S, Sand, A, Biterova, E.I, Barycki, J.J. | Deposit date: | 2008-12-25 | Release date: | 2009-05-19 | Last modified: | 2017-11-01 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Crystal Structure of Acivicin-Inhibited gamma-Glutamyltranspeptidase Reveals Critical Roles for Its C-Terminus in Autoprocessing and Catalysis. Biochemistry, 48, 2009
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2NQO
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![BU of 2nqo by Molmil](/molmil-images/mine/2nqo) | Crystal Structure of Helicobacter pylori gamma-Glutamyltranspeptidase | Descriptor: | Gamma-glutamyltranspeptidase | Authors: | Boanca, G, Sand, A, Okada, T, Suzuki, H, Kumagai, H, Fukuyama, K, Barycki, J.J. | Deposit date: | 2006-10-31 | Release date: | 2006-11-21 | Last modified: | 2023-08-30 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad. J.Biol.Chem., 282, 2007
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