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Results 1 - 7 of 7
EC Number Crystallization (Commentary)
Show all pathways known for 3.4.11.2Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.2-
Show all pathways known for 3.4.11.2Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.2in complex with inhibitors [1-amino-2-(cyclohexylamino)ethyl]phosphonic acid and (1-amino-2-anilinoethyl)phosphonic acid
Show all pathways known for 3.4.11.2Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.2in complex with the amino acids L-arginine, L-lysine, L-phenylalanine, L-tryptophan, and L-tyrosine, hanging drop vapour diffusion method
Show all pathways known for 3.4.11.2Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.2ligand-free protein and complex with bestatin at 1.5 and 1.6 A resolution, respectively. The enzyme is composed of an N-terminal beta-domain, a catalytic domain, a middle beta-domain, and a C-terminal alpha-domain. Residues E298 and Y381 located near the zinc ion, are involved in peptide cleavage. Residue M260 functions as a cushion to accept substrates with different N-terminal resiude sizes
Show all pathways known for 3.4.11.2Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.2modeling of docking of 3-galloylamido-N-substituted-2,6-piperidinedione-N-acetamide inhibitors
Show all pathways known for 3.4.11.2Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.2selenomethionine labeled protein, to 2.05 A resolution. Enzyme is composed of the N-terminal domain I, the catalytic domain II, domain III, and the C-terminal domain IV
Show all pathways known for 3.4.11.2Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.2to 2.0 A resolution, space group P3121
Results 1 - 7 of 7