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EC Number Crystallization (Commentary) Reference
Show all pathways known for 2.4.2.1Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.1- 489651, 489657, 489676, 489688, 489708, 671065
Show all pathways known for 2.4.2.1Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.12.24 A resolution 660620
Show all pathways known for 2.4.2.1Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.1analysis of the structures of MTI (PDB ID 1Q1G) and DADMe-I (PDB ID 3PHC) co-crystallized with the protein structure of PfPNP 759775
Show all pathways known for 2.4.2.1Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.1binary complex of the trimeric enzyme with the potent ground-state analog inhibitor 9-(5,5-difluoro-5-phosphonopentyl)guanine crystallized in the cubic space group P2(1)3 with unit-cell parameter a = 93.183 A 660583
Show all pathways known for 2.4.2.1Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.1calorimetric titration of recombinant calf PNP complexed with immucillin H. Stoichiometry shows three immucillin molecules per enzyme trimer, enzyme does not show negative cooperativity. One-third-of-the-sites binding does not occur for trimeric enzyme 721842
Show all pathways known for 2.4.2.1Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.1cocrystallization of L-immucillin-H and 4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-H with the enzyme and phosphate. The structures with L-immucillin-H and 4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-H are solved to 2.9 A and 2.1 A resolution, respectively 687308
Show all pathways known for 2.4.2.1Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.1complex of enzyme with hypoxanthine at 2.15 A resolution, structural data from crystal structure may be useful in designing prodrugs that can be activated by Escherichia coli enzyme but not the human enzyme 489700
Show all pathways known for 2.4.2.1Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.1conformational states in complex with transition state analogues Immucillin-H and DATMe-Immucillin-H. The (purine nucelotide phosphorylase)3(PO4)3 ImmH-complex is more compact by sedimentation rate than the other complexes. Purine nucelotide phosphorylase protein conformation of dynamic motion correlates more closely with entropy of binding than with affinity. Catalytically active turnover with saturated substrate sites causes less change in peptide amide deuterium exchange and sedimentation rates than binding of transition state analogues. DATMe-Immucilin-H more closely mimics the transition of human PNP than does Immucilin-H and achieves strong binding interactions at the catalytic site while causing relatively modest alterations of the protein dynamic motion 702365
Show all pathways known for 2.4.2.1Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.1construction of three-dimensional model 722143
Show all pathways known for 2.4.2.1Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.1crystal structure of AgPNP is determined in complex with 5'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-H and phosphate to a resolution of 2.2 A 685103
Results 1 - 10 of 52 > >>