1BHS
HUMAN ESTROGENIC 17BETA-HYDROXYSTEROID DEHYDROGENASE
Summary for 1BHS
Entry DOI | 10.2210/pdb1bhs/pdb |
Descriptor | 17BETA-HYDROXYSTEROID DEHYDROGENASE (2 entities in total) |
Functional Keywords | short-chain dehydrogenase, steroid dehydrogenase, estrogen, human type i 17beta-hsd, human placental 17beta-hsd, oxidoreductase |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm: P14061 |
Total number of polymer chains | 1 |
Total formula weight | 34887.83 |
Authors | Ghosh, D. (deposition date: 1995-04-19, release date: 1996-12-07, Last modification date: 2024-02-07) |
Primary citation | Ghosh, D.,Pletnev, V.Z.,Zhu, D.W.,Wawrzak, Z.,Duax, W.L.,Pangborn, W.,Labrie, F.,Lin, S.X. Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution. Structure, 3:503-513, 1995 Cited by PubMed Abstract: The principal human estrogen, 17 beta-estradiol, is a potent stimulator of certain endocrine-dependent forms of breast cancer. Because human estrogenic 17 beta-hydroxysteroid dehydrogenase (type I 17 beta-HSD) catalyzes the last step in the biosynthesis of 17 beta-estradiol from the less potent estrogen, estrone, it is an attractive target for the design of inhibitors of estrogen production and tumor growth. This human enzyme shares less than 15% sequence identity with a bacterial 3 alpha,20 beta-HSD, for which the three-dimensional structure is known. The amino acid sequence of 17 beta-HSD also differs from that of bacterial 3 alpha,20 beta-HSD by two insertions (of 11 and 14 residues) and 52 additional residues at the C terminus. PubMed: 7663947DOI: 10.1016/S0969-2126(01)00183-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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