   3.7.1.14 | hanging-drop vapour-diffusion method. The 2.1 A resolution X-ray structure of the native enzyme determined from orthorhombic crystals confirms that it is a member of the alpha/beta hydrolase fold family, comprising eight beta-strands interconnected by loops and helices. The 2.8 A resolution structure of the enzyme cocrystallized with the non-hydrolysable substrate analogue 2,6-diketo-nona-1,9-dioic acid confirms the location of the active site in a buried channel including Ser110, His263 and Asp235, postulated contributors to a serine protease-like catalytic triad in homologous enzymes |
