3FNM
Crystal structure of acivicin-inhibited gamma-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis
Summary for 3FNM
Entry DOI | 10.2210/pdb3fnm/pdb |
Related | 2NQO 2QMG |
Descriptor | Gamma-glutamyltranspeptidase (Ggt) Large subunit, Gamma-glutamyltranspeptidase (Ggt) Small subunit, (2S)-AMINO[(5S)-3-CHLORO-4,5-DIHYDROISOXAZOL-5-YL]ACETIC ACID, ... (4 entities in total) |
Functional Keywords | ntn-hydrolase, glutamyltranspeptidase, transferase |
Biological source | Helicobacter pylori (Campylobacter pylori) More |
Total number of polymer chains | 4 |
Total formula weight | 122332.28 |
Authors | Williams, K.,Cullati, S.,Sand, A.,Biterova, E.I.,Barycki, J.J. (deposition date: 2008-12-25, release date: 2009-05-19, Last modification date: 2017-11-01) |
Primary citation | Williams, K.,Cullati, S.,Sand, A.,Biterova, E.I.,Barycki, J.J. Crystal Structure of Acivicin-Inhibited gamma-Glutamyltranspeptidase Reveals Critical Roles for Its C-Terminus in Autoprocessing and Catalysis. Biochemistry, 48:2459-2467, 2009 Cited by PubMed: 19256527DOI: 10.1021/bi8014955 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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