1FDS
HUMAN 17-BETA-HYDROXYSTEROID-DEHYDROGENASE TYPE 1 COMPLEXED WITH 17-BETA-ESTRADIOL
Summary for 1FDS
Entry DOI | 10.2210/pdb1fds/pdb |
Descriptor | 17-BETA-HYDROXYSTEROID-DEHYDROGENASE, ESTRADIOL (3 entities in total) |
Functional Keywords | dehydrogenase, 17-beta-hydroxysteroid |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm: P14061 |
Total number of polymer chains | 1 |
Total formula weight | 35246.33 |
Authors | Housset, D.,Breton, R.,Mazza, C.,Fontecilla-Camps, J.-C. (deposition date: 1996-06-28, release date: 1997-02-12, Last modification date: 2024-04-03) |
Primary citation | Breton, R.,Housset, D.,Mazza, C.,Fontecilla-Camps, J.C. The structure of a complex of human 17beta-hydroxysteroid dehydrogenase with estradiol and NADP+ identifies two principal targets for the design of inhibitors. Structure, 4:905-915, 1996 Cited by PubMed Abstract: The steroid hormone 17beta-estradiol is important in the genesis and development of human breast cancer. Its intracellular concentration is regulated by 17beta-hydroxysteroid dehydrogenase, which catalyzes the reversible reduction of estrone to 17beta-estradiol. This enzyme is thus an important target for inhibitor design. The precise localization and orientation of the substrate and cofactor in the active site is of paramount importance for the design of such inhibitors, and for an understanding of the catalytic mechanism. PubMed: 8805577DOI: 10.1016/S0969-2126(96)00098-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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