Enoyl-CoA hydratase catalyses the conversion of (3S)-3-Hydroxyacyl-CoA to trans-2,3-Dehydroacyl-CoA + H2O, the second step in the fatty acid metabolic pathway. A plethora of homologs to this Bacillus anthracis protein have been structurally characterized. Similar to many of the homologs, the hexameric biological unit is observed within the crystal’s asymmetric unit. The Enoyl-CoA hydratase monomer is also similar to previously reported structures. Each monomer consists of a larger globular N-terminal domain and a smaller α-helical C-terminal domain. The C-terminal domain extends away from the globular core to interact with several adjacent molecules in the biological hexamer. The active site lies in a cavity between one molecule’s N-terminal globular core and an adjacent molecule’s C-terminal α-helical domain.