EC Number   |
|---|
   3.4.17.2 | - |
| 3.4.17.2 | crystal structures of selenium-, sulfur-, and phosphinic acid containing inhibitors bound to porcine pancreatic carboxypeptidase B are determined at 1.7, 2.15 and 1.9 A, respectively |
| 3.4.17.2 | crystals of porcine pancreatic carboxypeptidase B are grown by the capillary counter-diffusion method in the presence of polyethylene glycol and zinc acetate. The three-dimensional structure of carboxypeptidase B is determined at 1.40 A resolution. The structure contains five zinc atoms, two of which are present in the active site of the enzyme, and an acetate ion |
| 3.4.17.2 | crystals of the complex of carboxypeptidase B and N-sulfamoyl-L-arginine are grown in a capillary in microgravity using the counter-diffusion technique. Crystals are grown in a form belonging to the same space group, P4(1)2(1)2, as the uncomplexed enzyme. X-ray data are collected to a resolution of 1.25 A |
| 3.4.17.2 | enzyme in complex with inhibitors DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid, 2-(5-carbamimidamido-2-chlorophenyl)-3-sulfanylpropanoic acid, (2R)-2-(3-carbamimidamidophenyl)-3-sulfanylpropanoic acid, or 5-carbamimidamido-2-(sulfanylmethyl)pentanoic acid, hanging drop vapour diffusion method, 0.21 mg/ml protein in 10 mM Tris, pH 7.0, 1 mM inhibitor, and 50 mM NaCl, mixed with an equal volume of 0.002 ml of reservoir solution containing 0.15-0.30 M magnesium acetate, 0.1 M sodium cacodylate, pH 6.5, and 12-22% PEG 8000, X-ray diffraction structure determination and analysis at 1.4-2.0 A resolution |
| 3.4.17.2 | recombinant enzyme in complex with tick carboxypeptidase inhibitor, sitting drop vapour diffusion method, mixing of equal volumes of protein and reservoir solutions, the latter containing 0.1 M bis-Tris. pH 5.5, 0.2 M lithium sulfate monohydrate, and 25% w/v PEG 3350, a few weeks at 20°C, X-ray diffraction structure determination and analysis at 2.0 A resolution |
| 3.4.17.2 | structure of the complex of the enzyme with a transition state analog N-sulfamoyl-L-phenylalanine solved at 1.74 A. Crystals of the enzyme/N-sulfamoyl-L-phenylalanine complex are grown in a capillary in microgravity using the counter-diffusion technique |
