2QMC
Crystal Structure of Helicobacter Pylori Gamma-Glutamyltranspeptidase T380A Mutant
Summary for 2QMC
Entry DOI | 10.2210/pdb2qmc/pdb |
Related | 2NQO 2QM6 |
Descriptor | Gamma-glutamyltranspeptidase, S-(P-NITROBENZYL)GLUTATHIONE, ... (4 entities in total) |
Functional Keywords | ntn-hydrolase, glutamyltranspeptidase, transferase |
Biological source | Helicobacter pylori More |
Total number of polymer chains | 4 |
Total formula weight | 122799.97 |
Authors | Barycki, J.J.,Boanca, G.,Sand, A. (deposition date: 2007-07-15, release date: 2008-02-12, Last modification date: 2023-08-30) |
Primary citation | Morrow, A.L.,Williams, K.,Sand, A.,Boanca, G.,Barycki, J.J. Characterization of Helicobacter pylori gamma-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis. Biochemistry, 46:13407-13414, 2007 Cited by PubMed: 17960917DOI: 10.1021/bi701599e PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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