1DJP
CRYSTAL STRUCTURE OF PSEUDOMONAS 7A GLUTAMINASE-ASPARAGINASE WITH THE INHIBITOR DON COVALENTLY BOUND IN THE ACTIVE SITE
Summary for 1DJP
Entry DOI | 10.2210/pdb1djp/pdb |
Related | 1DJO 4PGA |
Descriptor | GLUTAMINASE-ASPARAGINASE, 5,5-dihydroxy-6-oxo-L-norleucine (3 entities in total) |
Functional Keywords | pga, glutaminase, asparaginase, don, 6-diazo-5-oxo-l-norvaline, glutaminase-asparaginase, suicide inhibitor, covalently bound inhibitor, hydrolase |
Biological source | Pseudomonas sp. |
Cellular location | Periplasm: P10182 |
Total number of polymer chains | 2 |
Total formula weight | 71146.36 |
Authors | Ortlund, E.,Lacount, M.W.,Lewinski, K.,Lebioda, L. (deposition date: 1999-12-03, release date: 2000-01-24, Last modification date: 2017-10-04) |
Primary citation | Ortlund, E.,Lacount, M.W.,Lewinski, K.,Lebioda, L. Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu. Biochemistry, 39:1199-1204, 2000 Cited by PubMed: 10684596DOI: 10.1021/bi991797d PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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