2HSD

THE REFINED THREE-DIMENSIONAL STRUCTURE OF 3ALPHA,20BETA-HYDROXYSTEROID DEHYDROGENASE AND POSSIBLE ROLES OF THE RESIDUES CONSERVED IN SHORT-CHAIN DEHYDROGENASES

Replaces:  1HSD

Summary for 2HSD

• Entry DOI: 10.2210/pdb2hsd/pdb
• Descriptor: 3-ALPHA, 20 BETA-HYDROXYSTEROID DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (2 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Streptomyces exfoliatus
• Total number of polymer chains: 4
• Total formula weight: 107760.08

Authors

Ghosh, D.,Duax, W.L. (deposition date: 1994-03-28, release date: 1994-08-31, Last modification date: 2024-02-14)

Primary citation

Ghosh, D.,Wawrzak, Z.,Weeks, C.M.,Duax, W.L.,Erman, M.
The refined three-dimensional structure of 3 alpha,20 beta-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases.
Structure, 2:629-640, 1994

PubMed Abstract: Bacterial 3 alpha,20 beta-hydroxysteroid dehydrogenase reversibly oxidizes the 3 alpha and 20 beta hydroxyl groups of steroids derived from androstanes and pregnanes. It was the first short-chain dehydrogenase to be studied by X-ray crystallography. The previous description of the structure of this enzyme, at 2.6 A resolution, did not permit unambiguous assignment of several important groups. We have further refined the structure of the complex of the enzyme with its cofactor, nicotinamide adenine dinucleotide (NAD), and solvent molecules, at the same resolution.

PubMed: 7922040
DOI: 10.1016/S0969-2126(00)00064-2

Experimental method

X-RAY DIFFRACTION (2.64 Å)