Glycerol-3-phosphate dehydrogenase is an NADH dependent enzyme which catalyzes the reduction of dihydroxyacetone to glycerol-3-phosphate. The enzyme has variety of biological functions, including maintenance of the NADH/NAD+ balance, a role in glucose glycolysis pathway, and prevention of build-up of the toxic compound methylglyoxylate. The Coxiella burnetii enzyme’s biological homodimer is observed within the crystal’s asymmetric unit. Each monomer consists of and N-terminal NAD-binding domain and a C-terminal substrate-binding domain. While the enzyme is structurally similar to previously characterized homologs (PDB code 1N1E), one difference from some homologs is the truncation of the C-terminus. In homologs, the C-terminus is observed to form a portion of the dimer interface. The absence of these residues in the Coxiella burnetii enzyme results in a reduced protein-protein interactions.