During crystallization screenings of commercially available hydrolytic enzymes, the new, hexagonal crystal form of CAL-B, has been discovered and hereby reported. The NAG molecules, which were closing the glycosylation site in the orthorhombic form, in hexagonal structure make the glycosylation site open. It is unknown whether the opening and closing of the glycosylation site by the 'lid' NAG molecules, could be related to the opening and closing of the active center of the enzyme upon substrate binding and product release.
        
Representative scheme of Canar_LipB structure and an image from PDBsum server
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Databases
PDB-Sum
4ZV7 Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
4ZV7Fold classification based on Structure-Structure alignment of Proteins - FSSP server