3GTU

LIGAND-FREE HETERODIMERIC HUMAN GLUTATHIONE S-TRANSFERASE M2-3 (EC 2.5.1.18), MONOCLINIC CRYSTAL FORM

Summary for 3GTU

DescriptorGLUTATHIONE S-TRANSFERASE (3 entities in total)
Functional Keywordstransferase, glutathione, conjugation, detoxification, cytosolic, heterodimer
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm P28161 P21266
Total number of polymer chains4
Total molecular weight104211.73
Authors
Patskovsky, Y.V.,Patskovska, L.N.,Listowsky, I. (deposition date: 1998-07-29, release date: 1999-07-29, Last modification date: 2011-07-13)
Primary citation
Patskovsky, Y.V.,Patskovska, L.N.,Listowsky, I.
An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases.
Biochemistry, 38:16187-16194, 1999
PubMed: 10587441 (PDB entries with the same primary citation)
DOI: 10.1021/bi991714t
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.8 Å)
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers70.7%2.9%3.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution