1gsc | pdb_00001gsc
From Proteopedia
NEW CRYSTAL FORMS OF A MU CLASS GLUTATHIONE S-TRANSFERASE FROM RAT LIVER
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Structural highlights
Function[GSTM1_RAT] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTwo new crystal forms of isoenzyme 3-3 of rat liver glutathione S-transferase (GST 3-3) have been obtained. They were grown under essentially the same crystallization conditions as those reported for the C2 crystal form [Fu, Rose, Chung, Tam & Wang (1991). Acta Cryst. B47, 813-814]. The new crystals belong to space group P2(1) with one form having cell dimensions a = 101.6, b = 69.5, c = 81.4 A, and beta = 113.6 degrees, and the other form having cell parameters a = 97.4, b = 81.1, c = 69.4 A and beta = 109.2 degrees. These new crystals diffract to at least 2.5 A, resolution. The molecular packing arrangements in these P2(1) crystals have been found by molecular replacement studies. New crystal forms of a micro-class glutathione S-transferase from rat liver.,Fu JH, Rose J, Tam MF, Wang BC Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):219-24. PMID:15299462[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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