1.1.1.B57	crystal structure of both wild-type and cobalt-substituted enzyme at 1.75 A and 2.20 A resolution, respectively. One metal ion per monomer is present only at the structural site. The co-crystal structure of the NADPH-bound form of the enzyme at 2.35 A resolution shows close structural conservation with horse ADH, despite the lack of a catalytic Zn2+. Modeling of 1-tetralone into the NADPH-bound structure suggests an arginine as a possible catalytic residue	728605