Crystal structure of the Selenocysteine to Cysteine Mutant of human phospholipid hydroperoxide glutathione peroxidase (GPx4)

Summary for 2OBI

DescriptorPhospholipid hydroperoxide glutathione peroxidase (GPX4) (2 entities in total)
Functional Keywordshuman gpx4, peroxidase, selenoprotein, thioredoxin-fold, anti-oxidatve defense system, oxidoreductase
Biological sourceHomo sapiens (human)
Cellular locationMitochondrion P36969
Total number of polymer chains1
Total molecular weight20955.08
Scheerer, P.,Krauss, N.,Hoehne, W. (deposition date: 2006-12-19, release date: 2007-09-18, Last modification date: 2011-07-13)
Primary citation
Scheerer, P.,Borchert, A.,Krauss, N.,Wessner, H.,Gerth, C.,Hohne, W.,Kuhn, H.
Structural basis for catalytic activity and enzyme polymerization of phospholipid hydroperoxide glutathione peroxidase-4 (GPx4).
Biochemistry, 46:9041-9049, 2007
PubMed: 17630701 (PDB entries with the same primary citation)
DOI: 10.1021/bi700840d
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliers0.225201.4%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

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