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Article

Hydrogen bonding at the active site of delta 5-3-ketosteroid isomerase.

Biochemistry - 2 Dec 1997

Zhao Q, Abeygunawardana C, Gittis A G, Mildvan A S

Abstract excerpt

The solution secondary structure of the highly active Y55F/Y88F "Tyr-14-only" mutant of delta 5-3-ketosteroid isomerase complexed with 19-nortestosterone hemisuccinate has been shown to consist of three helices, a six-stranded mixed beta-sheet, and five turns. The steroid binds near the general acid, Tyr-14, on helix 1, near the general base, Asp-38, on the first strand of the beta-sheet, and on the hydrophobic...

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Identifiers

PMID: 9398180
DOI: 10.1021/bi971549m

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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