Entry Database : PDB / ID : 5s55 Structure visualization Downloads & linksTitle Tubulin-Z106307058-complex ComponentsStathmin-4 Tubulin alpha-1B chain Tubulin beta-2B chain Tubulin-Tyrosine Ligase DetailsKeywords CELL CYCLE / TUBULIN FOLD / CYTOSKELETON / MICROTUBULEFunction / homology Function and homology informationFunction Domain/homology Component
tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / microtubule-based process / regulation of microtubule polymerization or depolymerization / tubulin binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / spindle microtubule / structural constituent of cytoskeleton ... tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / microtubule-based process / regulation of microtubule polymerization or depolymerization / tubulin binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / spindle microtubule / structural constituent of cytoskeleton / microtubule cytoskeleton organization / microtubule cytoskeleton / neuron projection development / nervous system development / mitotic cell cycle / growth cone / microtubule / neuron projection / protein heterodimerization activity / nucleotide binding / GTPase activity / GTP binding / Golgi apparatus / metal ion binding / cytoplasm / cytosol Similarity search - Function Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Stathmin family / Stathmin, conserved site / Stathmin superfamily / Stathmin family / Stathmin family signature 1. / Stathmin family signature 2. / Stathmin-like (SLD) domain profile. ... Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Stathmin family / Stathmin, conserved site / Stathmin superfamily / Stathmin family / Stathmin family signature 1. / Stathmin family signature 2. / Stathmin-like (SLD) domain profile. / Tubulin-beta mRNA autoregulation signal. / Alpha tubulin / Beta tubulin, autoregulation binding site / Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily Similarity search - Domain/homology PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Chem-WZP / Tubulin tyrosine ligase / Stathmin-4 / Tubulin alpha-1B chain / Tubulin beta-2B chain Similarity search - ComponentBiological species Rattus norvegicus (Norway rat)Gallus gallus (chicken)Bos taurus (cattle)Method X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution : 2.3 Å DetailsAuthors Muehlethaler, T. / Gioia, D. / Prota, A.E. / Sharpe, M.E. / Cavalli, A. / Steinmetz, M.O. Funding support European Union, Italy, Switzerland, 4items Details Hide detailsOrganization Grant number Country iNEXT/Horizon 2020 PID2692 European Union NEON/Regione Lombardia ID239047 Italy Swiss National Science Foundation 31003A_166608 Switzerland Swiss National Science Foundation 31030A_192566 Switzerland
CitationJournal : Angew.Chem.Int.Ed.Engl. / Year : 2021Title : Comprehensive Analysis of Binding Sites in Tubulin.Authors : Muhlethaler, T. / Gioia, D. / Prota, A.E. / Sharpe, M.E. / Cavalli, A. / Steinmetz, M.O. History Deposition Nov 8, 2020 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Jun 30, 2021 Provider : repository / Type : Initial releaseRevision 1.1 Mar 6, 2024 Group : Advisory / Data collection / Database referencesCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_unobs_or_zero_occ_atoms Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession
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