The psychrophilic enzyme is an interesting subject to study due to its special ability to adapt to extreme temperatures, unlike typical enzymes. Previously, we have isolated a cold active lipase (AMS8 lipase) from an Antarctic Pseudomonas sp. The enzyme was successfully expressed  in E.coli expression system and purified to homogeneity. The structure and function of the cold active family I.3 lipase was predicted utilizing computer-aided software. Molecular dynamic simulation is performed at different temperatures for structural flexibility and stability analysis. The results show that the enzyme is most stable at 0ºC and 5ºC. In terms of stability and flexibility, the catalytic domain (N-terminus) maintained its stability than the non-catalytic domain (C-terminus), but the non-catalytic domain showed higher flexibility than the catalytic domain. The analysis of the structure and function of AMS lipase provides new insights into the structural adaptation of this protein at low temperatures. The information obtained could be a useful tool for low temperature organic synthesis and molecular engineering purposes, in the near future.