Entry | Database: PDB / ID: 2c7s |
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Title | Crystal structure of human protein tyrosine phosphatase kappa at 1.95A resolution |
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Components | RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE KAPPA |
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Keywords | HYDROLASE / RECEPTOR TYPE TYROSINE PHOSPHATASE KAPPA / PTPRK / GLYCOPROTEIN / IMMUNOGLOBULIN DOMAIN / PROTEIN PHOSPHATASE / RECEPTOR / TRANSMEMBRANE |
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Function / homology | Function and homology information
gamma-catenin binding / transmembrane receptor protein tyrosine phosphatase activity / leading edge membrane / focal adhesion assembly / protein localization to cell surface / negative regulation of cell cycle / negative regulation of keratinocyte proliferation / protein dephosphorylation / negative regulation of cell migration / protein-tyrosine-phosphatase ...gamma-catenin binding / transmembrane receptor protein tyrosine phosphatase activity / leading edge membrane / focal adhesion assembly / protein localization to cell surface / negative regulation of cell cycle / negative regulation of keratinocyte proliferation / protein dephosphorylation / negative regulation of cell migration / protein-tyrosine-phosphatase / transforming growth factor beta receptor signaling pathway / protein tyrosine phosphatase activity / adherens junction / EGFR downregulation / beta-catenin binding / cellular response to reactive oxygen species / cellular response to UV / cell-cell junction / cell migration / cell junction / cell adhesion / negative regulation of cell population proliferation / intracellular membrane-bounded organelle / negative regulation of DNA-templated transcription / protein kinase binding / cell surface / signal transduction / membrane / plasma membraneSimilarity search - Function MAM domain signature. / Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others) / MAM domain, meprin/A5/mu / MAM domain / MAM domain profile. / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / Protein tyrosine phosphatase, catalytic domain / PTP type protein phosphatase domain profile. / Immunoglobulin I-set ...MAM domain signature. / Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others) / MAM domain, meprin/A5/mu / MAM domain / MAM domain profile. / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / Protein tyrosine phosphatase, catalytic domain / PTP type protein phosphatase domain profile. / Immunoglobulin I-set / Immunoglobulin I-set domain / 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 / Fibronectin type III domain / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Concanavalin A-like lectin/glucanase domain superfamily / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / Alpha-Beta Complex / Alpha BetaSimilarity search - Domain/homology |
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Biological species | HOMO SAPIENS (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å |
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Authors | Debreczeni, J.E. / Ugochukwu, E. / Eswaran, J. / Barr, A. / Das, S. / Burgess, N. / Gileadi, O. / Longman, E. / von Delft, F. / Knapp, S. ...Debreczeni, J.E. / Ugochukwu, E. / Eswaran, J. / Barr, A. / Das, S. / Burgess, N. / Gileadi, O. / Longman, E. / von Delft, F. / Knapp, S. / Sundstron, M. / Arrowsmith, C. / Weigelt, J. / Edwards, A. |
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Citation | Journal: Protein Sci. / Year: 2006 Title: The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1. Authors: Eswaran, J. / Debreczeni, J.E. / Longman, E. / Barr, A.J. / Knapp, S. |
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History | Deposition | Nov 28, 2005 | Deposition site: PDBE / Processing site: PDBE |
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Revision 1.0 | Jan 2, 2007 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jul 13, 2011 | Group: Advisory / Version format compliance |
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Revision 1.2 | Jan 24, 2018 | Group: Structure summary / Category: audit_author / Item: _audit_author.name |
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Revision 1.3 | Feb 28, 2018 | Group: Database references / Source and taxonomy / Structure summary Category: citation / citation_author ...citation / citation_author / entity_src_gen / struct Item: _citation.page_last / _citation.pdbx_database_id_DOI ..._citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation_author.name / _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _struct.title |
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Revision 1.4 | May 8, 2019 | Group: Data collection / Derived calculations / Experimental preparation Category: exptl_crystal_grow / pdbx_struct_special_symmetry / Item: _exptl_crystal_grow.method |
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Revision 1.5 | Dec 13, 2023 | Group: Data collection / Database references ...Data collection / Database references / 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 Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf |
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