The 1.75 A resolution structure of the wild type IDP01880 protein was solved by molecular replacement using the structure of this protein (PDB ID 3N77) with three point mutations (K118A, E120A, E121A) as a model. It is interesting to note that both structures have different crystal packing, which might be a result of site-directed mutagenesis. Pairwise structural alignment clearly shows that the residues Lys188, Glu120 and Glu121 if not mutated would clash with the Leu63-Ile66 stretch of residues of symmetry related molecule in the 3N77 structure. Residues 25 through 30 in chain A of the 3OGA structure are disordered, whereas they are built in chain B. These residues constitute a loop, which conformation is different from that of the mutant structure. Additionally, residues 78 through 88 in chain B and residues 82-83 in chain A of the wild type structure are disordered.