2gtu

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File:2gtu.png

Template:STRUCTURE 2gtu

LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18), MONOCLINIC CRYSTAL FORMLIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18), MONOCLINIC CRYSTAL FORM

Template:ABSTRACT PUBMED 10652317

About this StructureAbout this Structure

2GTU is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}

↑ Patskovsky YV, Patskovska LN, Listowsky I. The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases. J Biol Chem. 2000 Feb 4;275(5):3296-304. PMID:10652317

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OCA

[1] Patskovsky YV, Patskovska LN, Listowsky I. The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases. J Biol Chem. 2000 Feb 4;275(5):3296-304. PMID:10652317

[xtra 1]