The hypothetical three-dimensional structure of the enzyme 1,3,4,6-tet
rachloro-1,4-cyclohexadiene hydrolase isolated from the strain Sfingom
onas paucimobilis UT26 was modelled. Hydrolytic dehalogenase from anot
her bacterial strain (Xanthobacter autotrophicus GJ10), previously stu
died by X-ray analysis, was used as a reference structure. Differences
between the residues in the active site cavity of both enzymes have b
een related to their substrate activity.