5hfk | pdb_00005hfk

CRYSTAL STRUCTURE OF A GLUTATHIONE S-TRANSFERASE PROTEIN FROM ESCHERICHIA COLI OCh 157:H7 STR. SAKAI (ECs3186, TARGET EFI-507414) WITH BOUND GLUTATHIONE

spinqualitylabelsall models 5hfk, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5hfk is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.551Å Ligands: GSH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function YFCG_ECOLI Exhibits a very robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the nucleophilic substrate. Is involved in defense against oxidative stress, probably via its peroxidase activity. See Also Glutathione S-transferase 3D structures

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