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Results 1 - 7 of 7
EC Number Crystallization (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.117analysis of crystal structure of KLK7: owing to the conformational restrictions of the relatively narrow S1 pocket, the formation of a stabilizing hydrogen bond between the P1-Tyr-OH and the carboxamide of Asn189 has to be mediated by a water molecule. The S2 subsite is less separated from the S4 subsite than in KLK4-6 and less limited in size owing to a different position of the His99 imidazole side chain, which may also contribute to the capacity for the adaptation to P2 side chains of various size 691153
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.117in complex with inhibitor 1-(2-chlorobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole. 2-Chlorobenzene inserts into the S1 pocket, the methyl group on the imidazoline ring is located at the S2 site composed of side chains of His99, Asp102, His57, and Ser214 753015
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.117kallikrein 7 bound to inhibitors succinyl-Ala-Ala-Pro-Phe-chloromethyl ketone and Ala-Ala-Phe-chloromethyl ketone, sitting-drop vapor diffusion method at 18°C, 0.001 ml protein solution, containing 7 mg/ml enzyme-inhibitor complex, is mixed with 0.001 ml reservoir solution containing 100 mM [bis(2-hydroxyethyl)amino]tris(hydroxymethyl)-methane-HCl, pH 6.0, 25% PEG 3350, and 2.5 M Li2SO4, equilibration against reservoir solution, X-ray diffraction structure determination and analysis at 1.0-2.5 A resolution 682553
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.117purified recombinant enzyme bound to specific inhibitor LEKTI domain 6, 8 mg/ml protein in sodium phosphate buffer, pH 7.5, with a reservoir solution containing 3.2 M ammonium sulfate in 0.1 M HEPES, pH 7.0, X-ray diffraction structure determination and anaylsis at 2.8 A resolution 683785
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.117purified recombinant His-tagged enzyme, sitting-drop vapour-diffusion method, 22°C, 0.0001 ml of 8 mg/ml protein in 50 mM sodium phosphate buffer, pH 7.5, mixed with 0.0001 ml of reservoir solution, X-ray diffraction structure determination and anaylsis at 2.8 A resolution 683032
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.117sitting drop vapour diffusion method, with 100 mM [bis(2-hydroxyethyl)amino]tris(hydroxymethyl)-methane-HCl, pH 6.0, 25% PEG 3350, and 2.5 M Li2SO4 or with 100 mM sodium cacodylate, pH 6.5, 200 mM magnesium acetate, and 30% (v/v) 2-methyl-2,4-pentanediol 682553
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.117two crystal structures of KLK7 are solved with either of two covalently bound chloromethyl ketone (CMK) inhibitors. Overall, the S1 pocket of KLK7 is larger and more hydrophobic than those of the tryptic KLK4, 5, and 6. The hydrophobicity of the S1 pocket is enhanced by the presence of Ala190 instead of Ser190, and at the bottom of the pocket, Asn189, a polar residue, replaces Asp189, a negatively charged residue. Consistent with specificity, Asn189 insteadof Asp189 would reduce the affinity of KLK7 for basic P1 side chains and allow binding of non-polar residues. The size and shape of the S1 pocket is well suited to accommodate residues with medium and large side chains, explaining the modified chymotryptic specificity. Tyr may be favored over Phe at P1 because of the potential of the carboxyamide group of Asn189 to hydrogen bond to a buried hydroxyl group 691153
Results 1 - 7 of 7