The Lipase Engeneering Database (LED) integrates information on sequence, structure and function of alpha/beta-hydrolases. This protein class is comprised of enzymes with various functions that share structural rather than sequence similarities. As part of updating the LED we analysed the structures of the proteins in the current version of the LED.
For these different architectures, features like the accessibility of the active centre are investigated. Furthermore collective movements of residues within alpha/beta-hydrolases are analysed by essential dynamics simulation to determine the movement of the identified modules. The overall goal is to set up a new architecture-based version of the Lipase Engineering Database and to characterise alpha/beta-hydrolases of each architecture type.