1ua5 | pdb_00001ua5

Non-fusion GST from S. japonicum in complex with glutathione

spinqualitylabelsall models 1ua5, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ua5 is a 1 chain structure with sequence from Schistosoma japonicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: GSH, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GST26_SCHJA Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. 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 Schistosoma japonicum glutathione S-transferase (SjGST) is a common fusion tag in recombinant protein production, and its 3-dimensional structure has been studied in the context of drug design. We have determined the crystal structure of non-fused SjGST complexed with glutathione, and compare it to complexes between glutathione and SjGST fusion proteins. Crystal structure of non-fused glutathione S-transferase from Schistosoma japonicum in complex with glutathione.,Kursula I, Heape AM, Kursula P Protein Pept Lett. 2005 Oct;12(7):709-12. doi: 10.2174/0929866054696154. PMID:16522189 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glutathione S-transferase 3D structures

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