Entry Database : PDB / ID : 4d3p Structure visualization Downloads & linksTitle crystal structure of point mutated DUSP19 (C150A) ComponentsDUAL SPECIFICITY PROTEIN PHOSPHATASE 19 Details Keywords HYDROLASE / DUSP19 / POINT MUTATIONFunction / homology Function and homology informationFunction Domain/homology Component
JUN kinase phosphatase activity / protein tyrosine/serine/threonine phosphatase activity / negative regulation of JUN kinase activity / MAP-kinase scaffold activity / negative regulation of JNK cascade / mitogen-activated protein kinase kinase kinase binding / myosin phosphatase activity / protein-serine/threonine phosphatase / protein kinase inhibitor activity / protein kinase activator activity ... JUN kinase phosphatase activity / protein tyrosine/serine/threonine phosphatase activity / negative regulation of JUN kinase activity / MAP-kinase scaffold activity / negative regulation of JNK cascade / mitogen-activated protein kinase kinase kinase binding / myosin phosphatase activity / protein-serine/threonine phosphatase / protein kinase inhibitor activity / protein kinase activator activity / positive regulation of protein kinase activity / positive regulation of JUN kinase activity / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity / positive regulation of JNK cascade / negative regulation of protein kinase activity / positive regulation of MAPK cascade / cytoplasm Similarity search - Function Dual specificity phosphatase, catalytic domain / Dual specificity phosphatase, catalytic domain / Dual specificity phosphatase, catalytic domain / Dual specificity protein phosphatase domain / Dual specificity protein phosphatase domain profile. / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / Tyrosine-specific protein phosphatases domain / Tyrosine specific protein phosphatases domain profile. / Protein-tyrosine phosphatase-like ... Dual specificity phosphatase, catalytic domain / Dual specificity phosphatase, catalytic domain / Dual specificity phosphatase, catalytic domain / Dual specificity protein phosphatase domain / Dual specificity protein phosphatase domain profile. / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / 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 : 1.27 Å DetailsAuthors Jeon, T.J. / Nam, K.T. / Ryu, S.E. CitationJournal : Biodesign / Year : 2015Title : Structural Analysis of Activity-Modulating Mutations of Dusp19Authors : Jeon, T.J. / Nam, K.T. / Ryu, S.E. History Deposition Oct 23, 2014 Deposition site : PDBE / Processing site : PDBERevision 1.0 Nov 4, 2015 Provider : repository / Type : Initial releaseRevision 1.1 Dec 20, 2023 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / 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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