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1BHS

HUMAN ESTROGENIC 17BETA-HYDROXYSTEROID DEHYDROGENASE

Summary for 1BHS
Entry DOI10.2210/pdb1bhs/pdb
Descriptor17BETA-HYDROXYSTEROID DEHYDROGENASE (2 entities in total)
Functional Keywordsshort-chain dehydrogenase, steroid dehydrogenase, estrogen, human type i 17beta-hsd, human placental 17beta-hsd, oxidoreductase
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: P14061
Total number of polymer chains1
Total formula weight34887.83
Authors
Ghosh, D. (deposition date: 1995-04-19, release date: 1996-12-07, Last modification date: 2024-02-07)
Primary citationGhosh, 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: 7663947
DOI: 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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数据于2025-06-18公开中

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