True lipases attach triacylglycerols and act at an oil-water interface; they constitute a ubiquitous group of enzymes catalysing a wide variety of reactions, many with industrial potential. But so far the three-dimensional structure has not been reported for any lipase. Here we report the X-ray structure of the Mucor miehei triglyceride lipase and describe the atomic model obtained at 3.1 A resolution and refined to 1.9 A resolution. It reveals a Ser..His..Asp trypsin-like catalytic triad with an active serine buried under a short helical fragment of a long surface loop.
        
Representative scheme of Lipase_3 structure and an image from PDBsum server
Databases
PDB-Sum
1TGL Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
1TGLFold classification based on Structure-Structure alignment of Proteins - FSSP server