Entry Database : PDB / ID : 6elw Structure visualization Downloads & linksTitle High resolution structure of selenocysteine containing human GPX4 ComponentsPhospholipid hydroperoxide glutathione peroxidase, mitochondrial Details Keywords OXIDOREDUCTASE / HUMAN GPX4 / PEROXIDASE / SELENOPROTEIN / THIOREDOXIN-FOLD / ANTI-OXIDATVE DEFENSE SYSTEMFunction / homology Function and homology informationFunction Domain/homology Component
phospholipid-hydroperoxide glutathione peroxidase / phospholipid-hydroperoxide glutathione peroxidase activity / Synthesis of 15-eicosatetraenoic acid derivatives / Synthesis of 12-eicosatetraenoic acid derivatives / negative regulation of ferroptosis / selenium binding / Synthesis of 5-eicosatetraenoic acids / glutathione peroxidase / lipoxygenase pathway / Biosynthesis of aspirin-triggered D-series resolvins ... phospholipid-hydroperoxide glutathione peroxidase / phospholipid-hydroperoxide glutathione peroxidase activity / Synthesis of 15-eicosatetraenoic acid derivatives / Synthesis of 12-eicosatetraenoic acid derivatives / negative regulation of ferroptosis / selenium binding / Synthesis of 5-eicosatetraenoic acids / glutathione peroxidase / lipoxygenase pathway / Biosynthesis of aspirin-triggered D-series resolvins / Biosynthesis of E-series 18(R)-resolvins / arachidonic acid metabolic process / Biosynthesis of D-series resolvins / Biosynthesis of E-series 18(S)-resolvins / glutathione peroxidase activity / long-chain fatty acid biosynthetic process / protein polymerization / phospholipid metabolic process / response to estradiol / chromatin organization / nuclear envelope / cellular response to oxidative stress / spermatogenesis / response to oxidative stress / protein-containing complex / mitochondrion / extracellular exosome / identical protein binding / nucleus / cytosol Similarity search - Function Glutathione peroxidase active site / Glutathione peroxidases active site. / Glutathione peroxidase / Glutathione peroxidase conserved site / Glutathione peroxidase / Glutathione peroxidases signature 2. / Glutathione peroxidase profile. / Glutaredoxin / Glutaredoxin / Thioredoxin-like superfamily ... Glutathione peroxidase active site / Glutathione peroxidases active site. / Glutathione peroxidase / Glutathione peroxidase conserved site / Glutathione peroxidase / Glutathione peroxidases signature 2. / Glutathione peroxidase profile. / Glutaredoxin / Glutaredoxin / Thioredoxin-like superfamily / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homologyBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.3 Å DetailsAuthors Kalms, J. / Borchert, A. / Kuhn, H. / Scheerer, P. Funding support Germany, 3items Details Hide detailsOrganization Grant number Country German Research Foundation SFB740 Germany German Research Foundation SFB1078 Germany German Research Foundation Ku961/11-1 Germany
CitationJournal : Biochim. Biophys. Acta / Year : 2018Title : Crystal structure and functional characterization of selenocysteine-containing glutathione peroxidase 4 suggests an alternative mechanism of peroxide reduction.Authors : Borchert, A. / Kalms, J. / Roth, S.R. / Rademacher, M. / Schmidt, A. / Holzhutter, H.G. / Kuhn, H. / Scheerer, P. History Deposition Sep 29, 2017 Deposition site : PDBE / Processing site : PDBERevision 1.0 Jun 20, 2018 Provider : repository / Type : Initial releaseRevision 1.1 Jul 4, 2018 Group : Data collection / Database references / Category : citationItem : _citation.journal_volume / _citation.page_first / _citation.page_lastRevision 1.2 Jan 17, 2024 Group : Data collection / Database references / Refinement descriptionCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession
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