3dgq | pdb_00003dgq

Crystal structure of the glutathione transferase PI enzyme in complex with the bifunctional inhibitor, etharapta

spinqualitylabelsall models 3dgq, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3dgq is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CL, EAA, MES, SO4 Related: 3dd3 Gene: GSTP1 (HUMAN) Activity: Glutathione transferase, with EC number 2.5.1.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GSTP1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. 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 PubMed Double trouble: A hybrid organic-inorganic (organometallic) inhibitor was designed to target glutathione transferases. The metal center is used to direct protein binding, while the organic moiety acts as the active-site inhibitor (see picture). The mechanism of inhibition was studied using a range of biophysical and biochemical methods. Rational design of an organometallic glutathione transferase inhibitor.,Ang WH, Parker LJ, De Luca A, Juillerat-Jeanneret L, Morton CJ, Lo Bello M, Parker MW, Dyson PJ Angew Chem Int Ed Engl. 2009;48(21):3854-7. PMID:19396894 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glutathione S-transferase

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