Entry Database : PDB / ID : 3zfd Structure visualization Downloads & linksTitle Crystal Structure of the Kif4 Motor Domain Complexed With Mg-AMPPNP ComponentsCHROMOSOME-ASSOCIATED KINESIN KIF4 Details Keywords HYDROLASE / MOLECULAR MOTOR / ATPASE / MICROTUBULEFunction / homology Function and homology informationFunction Domain/homology Component
Kinesins / mitotic spindle midzone assembly / Recycling pathway of L1 / COPI-dependent Golgi-to-ER retrograde traffic / spindle elongation / MHC class II antigen presentation / microtubule associated complex / microtubule motor activity / microtubule-based movement / iron-sulfur cluster binding ... Kinesins / mitotic spindle midzone assembly / Recycling pathway of L1 / COPI-dependent Golgi-to-ER retrograde traffic / spindle elongation / MHC class II antigen presentation / microtubule associated complex / microtubule motor activity / microtubule-based movement / iron-sulfur cluster binding / mitotic cytokinesis / mitotic spindle organization / chromosome / midbody / microtubule binding / microtubule / DNA binding / nucleoplasm / ATP binding / metal ion binding / cytosol Similarity search - Function Tesmin/TSO1-like CXC domain / Tesmin/TSO1-like CXC domain / Kinesin motor domain / Kinesin / Kinesin-like protein / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain / Kinesin motor domain profile. / Kinesin motor, catalytic domain. ATPase. ... Tesmin/TSO1-like CXC domain / Tesmin/TSO1-like CXC domain / Kinesin motor domain / Kinesin / Kinesin-like protein / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain / Kinesin motor domain profile. / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain / Kinesin motor domain superfamily / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homologyBiological species MUS MUSCULUS (house mouse)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.71 Å DetailsAuthors Chang, Q. / Nitta, R. / Inoue, S. / Hirokawa, N. CitationJournal : J.Mol.Biol. / Year : 2013Title : Structural Basis for the ATP-Induced Isomerization of Kinesin.Authors : Chang, Q. / Nitta, R. / Inoue, S. / Hirokawa, N. History Deposition Dec 11, 2012 Deposition site : PDBE / Processing site : PDBERevision 1.0 Mar 20, 2013 Provider : repository / Type : Initial releaseRevision 1.1 Apr 3, 2013 Group : Database referencesRevision 1.2 May 29, 2013 Group : Database referencesRevision 1.3 Dec 20, 2023 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / 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 / pdbx_struct_conn_angle / struct_conn / struct_site Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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.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.pdbx_dist_value / _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_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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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