1HDC
MECHANISM OF INHIBITION OF 3ALPHA,20BETA-HYDROXYSTEROID DEHYDROGENASE BY A LICORICE-DERIVED STEROIDAL INHIBITOR
Summary for 1HDC
Entry DOI | 10.2210/pdb1hdc/pdb |
Descriptor | 3-ALPHA, 20 BETA-HYDROXYSTEROID DEHYDROGENASE, CARBENOXOLONE (3 entities in total) |
Functional Keywords | oxidoreductase |
Biological source | Streptomyces exfoliatus |
Total number of polymer chains | 4 |
Total formula weight | 107845.81 |
Authors | Ghosh, D. (deposition date: 1994-10-21, release date: 1995-02-07, Last modification date: 2024-02-07) |
Primary citation | Ghosh, D.,Erman, M.,Wawrzak, Z.,Duax, W.L.,Pangborn, W. Mechanism of inhibition of 3 alpha, 20 beta-hydroxysteroid dehydrogenase by a licorice-derived steroidal inhibitor. Structure, 2:973-980, 1994 Cited by PubMed Abstract: Bacterial 3 alpha, 20 beta-hydroxysteroid dehydrogenase (3 alpha, 20 beta-HSD) reversibly oxidizes the 3 alpha and 20 beta hydroxyl groups of androstanes and pregnanes and uses nicotinamide adenine dinucleotide as a cofactor. 3 alpha, 20 beta-HSD belongs to a family of short-chain dehydrogenases that has a highly conserved Tyr-X-X-X-Lys sequence. The family includes mammalian enzymes involved in hypertension, digestion, fertility and spermatogenesis. Several members of the enzyme family, including 3 alpha, 20 beta-HSD, are competitively inhibited by glycyrrhizic acid, a steroidal compound found in licorice, and its derivative, carbenoxolone, an anti-inflammatory glucocorticoid. PubMed: 7866748DOI: 10.1016/S0969-2126(94)00099-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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