2GST

STRUCTURE OF THE XENOBIOTIC SUBSTRATE BINDING SITE OF A GLUTATHIONE S-TRANSFERASE AS REVEALED BY X-RAY CRYSTALLOGRAPHIC ANALYSIS OF PRODUCT COMPLEXES WITH THE DIASTEREOMERS OF 9-(S-GLUTATHIONYL)-10-HYDROXY-9, 10-DIHYDROPHENANTHRENE

Summary for 2GST

DescriptorGLUTATHIONE S-TRANSFERASE, SULFATE ION, L-gamma-glutamyl-S-[(9S,10S)-10-hydroxy-9,10-dihydrophenanthren-9-yl]-L-cysteinylglycine, ... (4 entities in total)
Functional Keywordsglutathione transferase
Biological sourceRattus rattus (black rat)
Cellular locationCytoplasm P04905
Total number of polymer chains2
Total molecular weight52832.81
Authors
Ji, X.,Armstrong, R.N.,Gilliland, G.L. (deposition date: 1993-06-07, release date: 1993-10-31, Last modification date: 2017-11-29)
Primary citation
Ji, X.,Johnson, W.W.,Sesay, M.A.,Dickert, L.,Prasad, S.M.,Ammon, H.L.,Armstrong, R.N.,Gilliland, G.L.
Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene.
Biochemistry, 33:1043-1052, 1994
PubMed: 8110735 (PDB entries with the same primary citation)
DOI: 10.1021/bi00171a002
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.8 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers100.2%7.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution