Entry Database : PDB / ID : 5sb9 Structure visualization Downloads & linksTitle Tubulin-maytansinoid-4a-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 / spindle microtubule / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / 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 / spindle microtubule / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / microtubule cytoskeleton / neuron projection development / mitotic cell cycle / nervous system development / 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. / Alpha tubulin / Tubulin-beta mRNA autoregulation signal. / 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 Chem-5IX / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / IMIDAZOLE / 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 / DIFFERENCE FOURIER / Resolution : 2.5 Å DetailsAuthors Marzullo, P. / Boiarska, Z. / Perez-Pena, H. / Abel, A.-C. / Alvarez-Bernad, B. / Lucena-Agell, D. / Vasile, F. / Sironi, M. / Steinmetz, M.O. / Prota, A.E. ...Marzullo, P. / Boiarska, Z. / Perez-Pena, H. / Abel, A.-C. / Alvarez-Bernad, B. / Lucena-Agell, D. / Vasile, F. / Sironi, M. / Steinmetz, M.O. / Prota, A.E. / Diaz, J.F. / Pieraccini, S. / Passarella, D. Funding support European Union, 1items Details Hide detailsOrganization Grant number Country H2020-MSCA-ITN-2019 860070 TUBINTRAIN European Union
CitationJournal : Chemistry / Year : 2022Title : Maytansinol Derivatives: Side Reactions as a Chance for New Tubulin Binders.Authors : Marzullo, P. / Boiarska, Z. / Perez-Pena, H. / Abel, A.C. / Alvarez-Bernad, B. / Lucena-Agell, D. / Vasile, F. / Sironi, M. / Altmann, K.H. / Prota, A.E. / Diaz, J.F. / Pieraccini, S. / Passarella, D. History Deposition Jul 20, 2021 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Dec 8, 2021 Provider : repository / Type : Initial releaseRevision 1.1 Feb 9, 2022 Group : Database references / Category : citationItem : _citation.journal_volume / _citation.page_first ... _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year Revision 2.0 Mar 9, 2022 Group : Advisory / Atomic model ... Advisory / Atomic model / Data collection / Database references / Derived calculations / Polymer sequence / Refinement description / Source and taxonomy / Structure summary Category : atom_site / atom_site_anisotrop ... atom_site / atom_site_anisotrop / diffrn_detector / diffrn_radiation_wavelength / diffrn_source / entity / entity_poly / entity_poly_seq / entity_src_gen / entity_src_nat / pdbx_contact_author / pdbx_deposit_group / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_refine_tls / pdbx_struct_conn_angle / pdbx_struct_sheet_hbond / pdbx_validate_close_contact / pdbx_validate_torsion / refine / refine_hist / refine_ls_shell / reflns / struct_conf / struct_conn / struct_mon_prot_cis / struct_ref_seq_dif Item : _diffrn_detector.pdbx_collection_date / _diffrn_radiation_wavelength.wavelength ... _diffrn_detector.pdbx_collection_date / _diffrn_radiation_wavelength.wavelength / _diffrn_source.pdbx_wavelength_list / _entity.formula_weight / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_poly_seq.mon_id / _entity_src_gen.gene_src_common_name / _entity_src_nat.common_name / _pdbx_contact_author.address_1 / _pdbx_contact_author.name_last / _pdbx_deposit_group.group_type / _pdbx_nonpoly_scheme.auth_seq_num / _pdbx_poly_seq_scheme.auth_mon_id / _pdbx_poly_seq_scheme.mon_id / _pdbx_poly_seq_scheme.pdb_mon_id / _pdbx_refine_tls.L[1][1] / _pdbx_refine_tls.L[1][2] / _pdbx_refine_tls.L[1][3] / _pdbx_refine_tls.L[2][2] / _pdbx_refine_tls.L[2][3] / _pdbx_refine_tls.L[3][3] / _pdbx_refine_tls.S[1][1] / _pdbx_refine_tls.S[1][2] / _pdbx_refine_tls.S[1][3] / _pdbx_refine_tls.S[2][1] / _pdbx_refine_tls.S[2][2] / _pdbx_refine_tls.S[2][3] / _pdbx_refine_tls.S[3][1] / _pdbx_refine_tls.S[3][2] / _pdbx_refine_tls.S[3][3] / _pdbx_refine_tls.T[1][1] / _pdbx_refine_tls.T[1][2] / _pdbx_refine_tls.T[1][3] / _pdbx_refine_tls.T[2][2] / _pdbx_refine_tls.T[2][3] / _pdbx_refine_tls.T[3][3] / _pdbx_refine_tls.origin_x / _pdbx_refine_tls.origin_y / _pdbx_refine_tls.origin_z / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _pdbx_struct_sheet_hbond.range_1_auth_comp_id / _pdbx_struct_sheet_hbond.range_1_auth_seq_id / _pdbx_struct_sheet_hbond.range_1_label_comp_id / _pdbx_struct_sheet_hbond.range_1_label_seq_id / _pdbx_struct_sheet_hbond.range_2_auth_comp_id / _pdbx_struct_sheet_hbond.range_2_auth_seq_id / _pdbx_struct_sheet_hbond.range_2_label_comp_id / _pdbx_struct_sheet_hbond.range_2_label_seq_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_atom_id_1 / _pdbx_validate_close_contact.auth_comp_id_1 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _pdbx_validate_close_contact.dist / _pdbx_validate_close_contact.label_alt_id_1 / _refine.B_iso_max / _refine.B_iso_mean / _refine.B_iso_min / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_obs / _refine.ls_number_reflns_R_free / _refine.ls_number_reflns_R_work / _refine.ls_number_reflns_obs / _refine.overall_SU_ML / _refine.pdbx_overall_phase_error / _refine_hist.number_atoms_total / _refine_hist.pdbx_B_iso_mean_ligand / _refine_hist.pdbx_B_iso_mean_solvent / _refine_hist.pdbx_number_atoms_protein / _refine_ls_shell.R_factor_R_free / _refine_ls_shell.R_factor_R_work / _reflns.number_obs / _reflns.pdbx_number_measured_all / _reflns.pdbx_redundancy / _struct_conf.end_auth_comp_id / _struct_conf.end_auth_seq_id / _struct_conf.end_label_comp_id / _struct_conf.end_label_seq_id / _struct_conf.pdbx_PDB_helix_length / _struct_conn.pdbx_dist_value / _struct_conn.ptnr2_auth_seq_id / _struct_mon_prot_cis.pdbx_omega_angle Revision 2.1 May 22, 2024 Group : Data collection / Category : chem_comp_atom / chem_comp_bond
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