Entry Database : PDB / ID : 7frr Structure visualization Downloads & linksTitle PanDDA analysis group deposition -- Crystal structure of PTP1B in complex with Z2856434906 ComponentsTyrosine-protein phosphatase non-receptor type 1 Details Keywords HYDROLASE / PanDDA / Diamond i24 fragment screening / protein tyrosine phosphatase / PTP / protein tyrosine phosphatase 1B / PTP1B / enzyme / allostery / multiconformerFunction / homology Function and homology informationFunction Domain/homology Component
regulation of hepatocyte growth factor receptor signaling pathway / PTK6 Down-Regulation / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / positive regulation of receptor catabolic process / insulin receptor recycling / negative regulation of PERK-mediated unfolded protein response / negative regulation of vascular endothelial growth factor receptor signaling pathway / regulation of intracellular protein transport / IRE1-mediated unfolded protein response / cytoplasmic side of endoplasmic reticulum membrane ... regulation of hepatocyte growth factor receptor signaling pathway / PTK6 Down-Regulation / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / positive regulation of receptor catabolic process / insulin receptor recycling / negative regulation of PERK-mediated unfolded protein response / negative regulation of vascular endothelial growth factor receptor signaling pathway / regulation of intracellular protein transport / IRE1-mediated unfolded protein response / cytoplasmic side of endoplasmic reticulum membrane / platelet-derived growth factor receptor-beta signaling pathway / sorting endosome / mitochondrial crista / positive regulation of IRE1-mediated unfolded protein response / regulation of type I interferon-mediated signaling pathway / regulation of endocytosis / non-membrane spanning protein tyrosine phosphatase activity / positive regulation of protein tyrosine kinase activity / peptidyl-tyrosine dephosphorylation / Regulation of IFNA/IFNB signaling / regulation of signal transduction / cellular response to unfolded protein / growth hormone receptor signaling pathway via JAK-STAT / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / negative regulation of signal transduction / Regulation of IFNG signaling / Growth hormone receptor signaling / MECP2 regulates neuronal receptors and channels / endoplasmic reticulum unfolded protein response / positive regulation of JUN kinase activity / Insulin receptor recycling / negative regulation of insulin receptor signaling pathway / ephrin receptor binding / Integrin signaling / protein dephosphorylation / protein-tyrosine-phosphatase / negative regulation of MAP kinase activity / protein phosphatase 2A binding / protein tyrosine phosphatase activity / endosome lumen / insulin receptor binding / Negative regulation of MET activity / negative regulation of ERK1 and ERK2 cascade / receptor tyrosine kinase binding / insulin receptor signaling pathway / actin cytoskeleton organization / early endosome / mitochondrial matrix / cadherin binding / protein kinase binding / enzyme binding / endoplasmic reticulum / protein-containing complex / RNA binding / zinc ion binding / cytoplasm / cytosol Similarity search - Function Protein-tyrosine phosphatase, non-receptor type-1/2 / Protein tyrosine phosphatase, catalytic domain / PTP type protein phosphatase domain profile. / Protein-tyrosine phosphatase / Tyrosine-specific protein phosphatase, PTPase domain / Protein-tyrosine phosphatase, catalytic / Protein tyrosine phosphatase, catalytic domain motif / Tyrosine specific protein phosphatases active site. / Protein-tyrosine phosphatase, active site / Tyrosine-specific protein phosphatases domain ... Protein-tyrosine phosphatase, non-receptor type-1/2 / Protein tyrosine phosphatase, catalytic domain / PTP type protein phosphatase domain profile. / Protein-tyrosine phosphatase / Tyrosine-specific protein phosphatase, PTPase domain / Protein-tyrosine phosphatase, catalytic / Protein tyrosine phosphatase, catalytic domain motif / Tyrosine specific protein phosphatases active site. / Protein-tyrosine phosphatase, active site / Tyrosine-specific protein phosphatases domain / Tyrosine specific protein phosphatases domain profile. / Protein-tyrosine phosphatase-like Similarity search - Domain/homologyBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution : 1.83 Å DetailsAuthors Mehlman, T. / Biel, J. / Azeem, S.M. / Nelson, E.R. / Hossain, S. / Dunnett, L.E. / Paterson, N.G. / Douangamath, A. / Talon, R. / Axford, D. ...Mehlman, T. / Biel, J. / Azeem, S.M. / Nelson, E.R. / Hossain, S. / Dunnett, L.E. / Paterson, N.G. / Douangamath, A. / Talon, R. / Axford, D. / Orins, H. / von Delft, F. / Keedy, D.A. Funding support United States, 2items Details Hide detailsOrganization Grant number Country U.S. Department of Education Graduate Assistance in Areas of National Need (GAANN) PA200A150068 United States National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) GM133769 United States
CitationJournal : Elife / Year : 2023Title : Room-temperature crystallography reveals altered binding of small-molecule fragments to PTP1B.Authors : Skaist Mehlman, T. / Biel, J.T. / Azeem, S.M. / Nelson, E.R. / Hossain, S. / Dunnett, L. / Paterson, N.G. / Douangamath, A. / Talon, R. / Axford, D. / Orins, H. / von Delft, F. / Keedy, D.A. History Deposition Oct 25, 2022 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Nov 23, 2022 Provider : repository / Type : Initial releaseRevision 1.1 Mar 29, 2023 Group : Database references / Category : citation / citation_authorItem : _citation.country / _citation.journal_abbrev ... _citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name Revision 1.2 May 22, 2024 Group : Data collection / Category : chem_comp_atom / chem_comp_bond
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