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EC Number Crystallization (Commentary) Reference
Show all pathways known for 4.2.1.24Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.24- 210733
Show all pathways known for 4.2.1.24Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.24crystal structure of enzyme complexed with 4-oxosebaic acid and of enzyme complexed with 4,7-dioxosebaic acid 652256
Show all pathways known for 4.2.1.24Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.24hanging drop method, enzyme complexed with the inhibitor laevulinic acid at 2.6 A resolution, unit cell parameters: a = 125.24 A, b = 125.24 A, c = 164.6 A and spec group P42(1)2 666028
Show all pathways known for 4.2.1.24Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.24hanging drop vapor-diffusion method. Crystal structures of the active site of Pseudomonas aeruginosa PBGS with the various inhibitors 5-hydroxylevulinic acid, 5,5'-oxybis(4-oxopentanoic acid), 5,5'-iminobis(4-oxopentanoic acid), 5,5'-thiobis(4-oxopentanoic acid), 5,5'-sulfinylbis(4-oxopentanoic acid) or 5,5'-sulfonylbis(4-oxopentanoic acid) 678204
Show all pathways known for 4.2.1.24Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.24hanging drop vapour diffusion method, crystals of the enzyme complex with levulinic acid solved at 1.67 A resolution, crystals belong to space group P42(1)2 with cell dimensions of a = b = 129.8 A, c = 86.7 A 664001
Show all pathways known for 4.2.1.24Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.24hanging-drop vapour diffusion method, X-ray structure of the enzyme in which the catalytic site of the enzyme is complexed with a putative cyclic intermediate composed of both substrate moieties, solved at 0.16 nm resolution 649757
Show all pathways known for 4.2.1.24Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.24high-resolution structure of the enzyme cocrystallized with a noncovalently bound moiety of the product, porphobilinogen. The pyrrole side-chain amino group is datively bound to the active-site zinc ion and the porphobilinogen carboxylates interact with the enzyme via hydrogen bonds and salt bridges with invariant residues. Comparison of substrate and product complexes from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis 746631
Show all pathways known for 4.2.1.24Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.24porphobilinogen synthase is cocrystallized with the alaremycin 701747
Show all pathways known for 4.2.1.24Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.24sitting-drop vapour-diffusion method 653303
Show all pathways known for 4.2.1.24Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.24structure of the active-site variant D139N of the Mg2+-dependent enzyme in complex with the inhibitor 5-fluorolevulinic acid 652890
Results 1 - 10 of 14 > >>