Entry Database : PDB / ID : 3egh Structure visualization Downloads & linksTitle Crystal structure of a complex between Protein Phosphatase 1 alpha (PP1), the PP1 binding and PDZ domains of Spinophilin and the small natural molecular toxin Nodularin-R ComponentsSerine/threonine-protein phosphatase PP1-alpha catalytic subunit Spinophilin nodularin R DetailsKeywords HYDROLASE/HYDROLASE INHIBITOR / PP1 / Serine/Threonine Phosphatase / Post Synaptic Density / Inhibitor / Carbohydrate metabolism / Cell cycle / Cell division / Glycogen metabolism / Hydrolase / Iron / Manganese / Metal-binding / Phosphoprotein / Protein phosphatase / Actin-binding / Cell junction / Cell projection / Cytoskeleton / Developmental protein / Differentiation / Neurogenesis / Nucleus / Synapse / HYDROLASE-HYDROLASE INHIBITOR COMPLEXFunction / homology Function and homology informationFunction Domain/homology Component
protein localization to actin cytoskeleton / positive regulation of protein localization to actin cortical patch / response to L-phenylalanine derivative / cytoplasmic side of dendritic spine plasma membrane / protein localization to cell periphery / cellular response to morphine / regulation of opioid receptor signaling pathway / developmental process involved in reproduction / response to prostaglandin E / response to kainic acid ... protein localization to actin cytoskeleton / positive regulation of protein localization to actin cortical patch / response to L-phenylalanine derivative / cytoplasmic side of dendritic spine plasma membrane / protein localization to cell periphery / cellular response to morphine / regulation of opioid receptor signaling pathway / developmental process involved in reproduction / response to prostaglandin E / response to kainic acid / regulation of glycogen catabolic process / reproductive system development / PTW/PP1 phosphatase complex / glycogen granule / regulation of glycogen biosynthetic process / cellular response to peptide / protein phosphatase 1 binding / cadherin binding involved in cell-cell adhesion / actin filament depolymerization / filopodium assembly / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / dendritic spine membrane / regulation of canonical Wnt signaling pathway / regulation of translational initiation / response to steroid hormone / protein phosphatase inhibitor activity / myosin phosphatase activity / cortical actin cytoskeleton / male mating behavior / positive regulation of protein localization / branching morphogenesis of an epithelial tube / protein serine/threonine phosphatase activity / glycogen metabolic process / dendritic spine neck / protein-serine/threonine phosphatase / dendritic spine head / dendrite development / Triglyceride catabolism / Maturation of hRSV A proteins / entrainment of circadian clock by photoperiod / phosphatase activity / phosphoprotein phosphatase activity / cellular response to organic cyclic compound / DARPP-32 events / response to immobilization stress / response to amino acid / D2 dopamine receptor binding / ribonucleoprotein complex binding / dephosphorylation / cellular response to epidermal growth factor stimulus / : / response to amphetamine / protein dephosphorylation / Downregulation of TGF-beta receptor signaling / learning / filopodium / cellular response to estradiol stimulus / hippocampus development / calcium-mediated signaling / actin filament organization / positive regulation of protein localization to plasma membrane / adherens junction / response to lead ion / regulation of protein phosphorylation / lung development / circadian regulation of gene expression / response to nicotine / regulation of circadian rhythm / response to organic cyclic compound / negative regulation of cell growth / cerebral cortex development / kinase binding / ruffle membrane / neuron projection development / actin filament binding / Circadian Clock / cell migration / actin cytoskeleton / cellular response to xenobiotic stimulus / presynapse / lamellipodium / response to estradiol / actin binding / growth cone / perikaryon / transmembrane transporter binding / nucleic acid binding / dendritic spine / postsynaptic density / protein kinase activity / response to xenobiotic stimulus / cell cycle / cell division / neuronal cell body / glutamatergic synapse / dendrite / protein-containing complex binding / nucleolus / extracellular exosome / nucleoplasm Similarity search - Function Neurabin-1/2, PDZ domain / Neurabin-like family / PDZ domain / Serine-threonine protein phosphatase, N-terminal / Serine-threonine protein phosphatase N-terminal domain / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / Metallo-dependent phosphatases / Purple Acid Phosphatase; chain A, domain 2 ... Neurabin-1/2, PDZ domain / Neurabin-like family / PDZ domain / Serine-threonine protein phosphatase, N-terminal / Serine-threonine protein phosphatase N-terminal domain / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / Metallo-dependent phosphatases / Purple Acid Phosphatase; chain A, domain 2 / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / PDZ domain / Metallo-dependent phosphatase-like / Pdz3 Domain / PDZ domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / 4-Layer Sandwich / Roll / Mainly Beta / Alpha Beta Similarity search - Domain/homologyBiological species Homo sapiens (human)Rattus norvegicus (Norway rat)Nodularia spumigena (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution : 2 Å DetailsAuthors Ragusa, M.J. / Page, R. / Peti, W. CitationJournal : Nat.Struct.Mol.Biol. / Year : 2010Title : Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites.Authors : Ragusa, M.J. / Dancheck, B. / Critton, D.A. / Nairn, A.C. / Page, R. / Peti, W. History Deposition Sep 10, 2008 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Mar 23, 2010 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Advisory / Atomic model ... Advisory / Atomic model / Database references / Derived calculations / Non-polymer description / Structure summary / Version format compliance Revision 1.2 Dec 12, 2012 Group : OtherRevision 1.3 Apr 10, 2013 Group : Derived calculationsRevision 1.4 Oct 25, 2017 Group : Advisory / Refinement description / Category : pdbx_validate_polymer_linkage / softwareRevision 2.0 Nov 15, 2023 Group : Atomic model / Data collection ... Atomic model / Data collection / Database references / Derived calculations Category : atom_site / chem_comp_atom ... atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / pdbx_validate_main_chain_plane / pdbx_validate_peptide_omega / struct_conn / struct_ref_seq_dif Item : _atom_site.auth_atom_id / _atom_site.label_atom_id ... _atom_site.auth_atom_id / _atom_site.label_atom_id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_value_order / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details
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