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Article

Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity.

Biochemistry - 21 Dec 2004

Gu Yijun, Guo Jianxia, Pal Ajay, Pan Su-Shu, Zimniak Piotr, Singh Shivendra V, Ji Xinhua

Abstract excerpt

The crystal structure of human class alpha glutathione (GSH) S-transferase A3-3 (hGSTA3-3) in complex with GSH was determined at 2.4 A. Despite considerable amino acid sequence identity with other human class alpha GSTs (e.g., hGSTA1-1), hGSTA3-3 is unique due to its exceptionally high steroid double bond isomerase activity for the transformation of Delta(5)-androstene-3,17-dione (Delta(5)-AD) to...

Topics

Amino Acid Substitution
Binding Sites
Computational Biology
Crystallography, X-Ray
Glutathione
Glutathione Transferase
Humans
Kinetics
Models, Molecular
Mutation
Steroid Isomerases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Steroids

Substrate Specificity

Source

Identifiers

PMID: 15595823
DOI: 10.1021/bi048757g

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-15595823-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity.PMID 15595823Read ↗

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