Entry Database : PDB / ID : 5sb3 Structure visualization Downloads & linksTitle Tubulin-todalam-4-complex ComponentsStathmin-4 Tubulin alpha-1B chain Tubulin beta-2B chain Tubulin-Tyrosine Ligase 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 / regulation of microtubule polymerization or depolymerization / microtubule-based process / 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 / regulation of microtubule polymerization or depolymerization / microtubule-based process / 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 / neuron projection development / microtubule cytoskeleton / 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 / cytosol / cytoplasm 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 N-[4-(2-anilino-1,3-thiazol-4-yl)phenyl]acetamide / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / 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 : 2.2 Å DetailsAuthors Muehlethaler, T. / Milanos, L. / Ortega, J.A. / Blum, T.B. / Gioia, D. / Prota, A.E. / Cavalli, A. / Steinmetz, M.O. Funding support Italy, Switzerland, 3items Details Hide detailsOrganization Grant number Country NEON/Regione Lombardia ID239047 Italy Swiss National Science Foundation 31003A_166608 Switzerland Swiss National Science Foundation 310030_192566 Switzerland
CitationJournal : Angew.Chem.Int.Ed.Engl. / Year : 2022Title : Rational Design of a Novel Tubulin Inhibitor with a Unique Mechanism of Action.Authors : Muhlethaler, T. / Milanos, L. / Ortega, J.A. / Blum, T.B. / Gioia, D. / Roy, B. / Prota, A.E. / Cavalli, A. / Steinmetz, M.O. History Deposition Jul 8, 2021 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Apr 27, 2022 Provider : repository / Type : Initial releaseRevision 1.1 May 11, 2022 Group : Database references / Category : citation / citation_authorItem : _citation.page_first / _citation.page_last ... _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID / _citation_author.name Revision 1.2 Jun 22, 2022 Group : Database references / Category : citation / Item : _citation.journal_volumeRevision 1.3 May 22, 2024 Group : Data collection / Category : chem_comp_atom / chem_comp_bond
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