Entry Database : PDB / ID : 2bge Structure visualization Downloads & linksTitle Structure-based design of Protein Tyrosine Phosphatase-1B Inhibitors ComponentsPROTEIN-TYROSINE PHOSPHATASE NON-RECEPTOR TYPE 1 Details Keywords HYDROLASE / PROTEIN TYROSINE PHOSPHATASE / 1 / 2 / 5-THIADIAZOLIDIN-3-ONE-1 / 1-DIOXIDE TEMPLATEFunction / homology Function and homology informationFunction Domain/homology Component
regulation of hepatocyte growth factor receptor signaling pathway / PTK6 Down-Regulation / positive regulation of receptor catabolic process / insulin receptor recycling / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / negative regulation of vascular endothelial growth factor receptor signaling pathway / negative regulation of PERK-mediated unfolded protein response / 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 / positive regulation of receptor catabolic process / insulin receptor recycling / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / negative regulation of vascular endothelial growth factor receptor signaling pathway / negative regulation of PERK-mediated unfolded protein response / 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 / MECP2 regulates neuronal receptors and channels / Growth hormone receptor signaling / endoplasmic reticulum unfolded protein response / positive regulation of JUN kinase activity / negative regulation of insulin receptor signaling pathway / Insulin receptor recycling / 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 / cytosol / cytoplasm Similarity search - Function Protein-tyrosine phosphatase, non-receptor type-1/2 / : / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / 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 ... Protein-tyrosine phosphatase, non-receptor type-1/2 / : / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / 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 / Alpha-Beta Complex / Alpha Beta Similarity search - Domain/homologyBiological species HOMO SAPIENS (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.8 Å DetailsAuthors Black, E. / Breed, J. / Breeze, A.L. / Embrey, K. / Garcia, R. / Gero, T.W. / Godfrey, L. / Kenny, P.W. / Morley, A.D. / Minshull, C.A. ...Black, E. / Breed, J. / Breeze, A.L. / Embrey, K. / Garcia, R. / Gero, T.W. / Godfrey, L. / Kenny, P.W. / Morley, A.D. / Minshull, C.A. / Pannifer, A.D. / Read, J. / Rees, A. / Russell, D.J. / Toader, D. / Tucker, J. CitationJournal : Bioorg.Med.Chem.Lett. / Year : 2005Title : Structure-Based Design of Protein Tyrosine Phosphatase-1B InhibitorsAuthors: Black, E. / Breed, J. / Breeze, A.L. / Embrey, K. / Garcia, R. / Gero, T.W. / Godfrey, L. / Kenny, P.W. / Morley, A.D. / Minshull, C.A. / Pannifer, A.D. / Read, J. / Rees, A. / Russell, D.J. ... Authors : Black, E. / Breed, J. / Breeze, A.L. / Embrey, K. / Garcia, R. / Gero, T.W. / Godfrey, L. / Kenny, P.W. / Morley, A.D. / Minshull, C.A. / Pannifer, A.D. / Read, J. / Rees, A. / Russell, D.J. / Toader, D. / Tucker, J. History Deposition Dec 21, 2004 Deposition site : PDBE / Processing site : PDBERevision 1.0 May 4, 2005 Provider : repository / Type : Initial releaseRevision 1.1 Oct 7, 2015 Group : Derived calculations / Non-polymer description ... Derived calculations / Non-polymer description / Other / Refinement description / Source and taxonomy / Version format compliance Revision 1.2 May 8, 2024 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / struct_site Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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