2c3q

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spinqualitylabelsall models 2c3q, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HUMAN GLUTATHIONE-S-TRANSFERASE T1-1 W234R MUTANT, COMPLEX WITH S-HEXYLGLUTATHIONE

Overview

The crystal structures of wild-type human theta class, glutathione-S-transferase (GST) T1-1 and its W234R mutant, where Trp234, was replaced by Arg, were solved both in the presence and absence of, S-hexyl-glutathione. The W234R mutant was of interest due to its, previously observed enhanced catalytic activity compared to the wild-type, enzyme. GST T1-1 from rat and mouse naturally contain Arg in position 234, with correspondingly high catalytic efficiency. The overall structure of, GST T1-1 is similar to that of GST T2-2, as expected from their 53%, sequence identity at the protein level. Wild-type GST T1-1 has the, side-chain of Trp234 occupying a significant portion of the active site., This bulky residue prevents efficient binding of both glutathione and, hydrophobic substrates ... [(full description)]

About this Structure

2C3Q is a [Single protein] structure of sequence from [Homo sapiens] with IOD and GTX as [ligands]. Active as [Glutathione transferase], with EC number [2.5.1.18]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structural basis of the suppressed catalytic activity of wild-type human glutathione transferase T1-1 compared to its W234R mutant., Tars K, Larsson AK, Shokeer A, Olin B, Mannervik B, Kleywegt GJ, J Mol Biol. 2006 Jan 6;355(1):96-105. Epub 2005 Nov 8. PMID:16298388

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