Entry Database : PDB / ID : 5e7u Structure visualization Downloads & linksTitle MBP-MamC loop structure, a magnetite biomineralizing protein from Magnetospirillium magneticum AMB-1 ComponentsMaltose-binding periplasmic protein,Tightly bound bacterial magnetic particle protein,Maltose-binding periplasmic protein Details Keywords Magnetite binding protein / Magnetite binding / mineralization / MBP / transport proteinFunction / homology Function and homology informationFunction Domain/homology Component
magnetosome membrane / detection of maltose stimulus / maltose transport complex / carbohydrate transport / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ATP-binding cassette (ABC) transporter complex ... magnetosome membrane / detection of maltose stimulus / maltose transport complex / carbohydrate transport / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / outer membrane-bounded periplasmic space / periplasmic space / DNA damage response / membrane / metal ion binding Similarity search - Function Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein Similarity search - Domain/homology alpha-maltose / Maltose/maltodextrin-binding periplasmic protein / Maltose/maltodextrin-binding periplasmic protein / Magnetosome protein MamC Similarity search - ComponentBiological species Escherichia coli (E. coli)Magnetospirillum magneticum AMB-1 (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 2.8 Å DetailsAuthors Nudelman, H. / Zarivach, R. CitationJournal : To Be Published Title : MBP-MamC loop structure, a magnetite biomineralizing protein from Magnetospirillium magneticum AMB-1Authors : Nudelman, H. / Zarivach, R. History Deposition Oct 13, 2015 Deposition site : RCSB / Processing site : PDBERevision 1.0 Mar 23, 2016 Provider : repository / Type : Initial releaseRevision 2.0 Jul 29, 2020 Group : Atomic model / Data collection ... Atomic model / Data collection / Derived calculations / Non-polymer description / Structure summary Category : atom_site / chem_comp ... atom_site / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / struct_asym / struct_conn / struct_site / struct_site_gen Item : _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ... _atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _struct_asym.entity_id Description : Carbohydrate remediation / Provider : repository / Type : RemediationRevision 2.1 Jan 10, 2024 Group : Data collection / Database references ... Data collection / Database references / Refinement description / Structure summary Category : chem_comp / chem_comp_atom ... chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item : _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
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