Entry Database : PDB / ID : 7r1h Structure visualization Downloads & linksTitle Crystal structure of a flavodiiron protein D52K mutant in the reduced state from Escherichia coli ComponentsAnaerobic nitric oxide reductase flavorubredoxin Details Keywords OXIDOREDUCTASE / flavodiiron / nitrosative stress / ROS / FMN / ironFunction / homology Function and homology informationFunction Domain/homology Component
nitric oxide reductase activity / oxidoreductase activity, acting on other nitrogenous compounds as donors / nitric oxide catabolic process / response to nitric oxide / FMN binding / electron transfer activity / oxidoreductase activity / iron ion binding / protein-containing complex / identical protein binding / cytoplasm Similarity search - Function Anaerobic nitric oxide reductase flavorubredoxin / Rubredoxin-oxygen oxidoreductase / ODP domain / ODP family beta lactamase / Rubredoxin domain / Rubredoxin / Rubredoxin-like domain / Rubredoxin-like domain profile. / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase ... Anaerobic nitric oxide reductase flavorubredoxin / Rubredoxin-oxygen oxidoreductase / ODP domain / ODP family beta lactamase / Rubredoxin domain / Rubredoxin / Rubredoxin-like domain / Rubredoxin-like domain profile. / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase / Flavodoxin / Flavodoxin-like domain profile. / Flavodoxin/nitric oxide synthase / Ribonuclease Z/Hydroxyacylglutathione hydrolase-like / Flavoprotein-like superfamily Similarity search - Domain/homology : / FLAVIN MONONUCLEOTIDE / ISOPROPYL ALCOHOL / OXYGEN ATOM / OXYGEN MOLECULE / Anaerobic nitric oxide reductase flavorubredoxin Similarity search - ComponentBiological species Escherichia coli K-12 (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.947 Å DetailsAuthors Borges, P.T. / Teixeira, M. / Romao, C.V. / Frazao, C. Funding support Portugal, 1items Details Hide detailsOrganization Grant number Country Foundation for Science and Technology (FCT) Portugal
CitationJournal : Acta Crystallogr D Struct Biol / Year : 2026Title : Structures of variants of Escherichia coli flavodiiron-type nitric oxide reductase reveal changes in the di-iron site.Authors : Borges, P.T. / Folgosa, F. / Martins, M.C. / Gotthard, G. / van der Linden, P. / Carpentier, P. / Teixeira, M. / Frazao, C. / Romao, C.V. History Deposition Feb 3, 2022 Deposition site : PDBE / Processing site : PDBERevision 1.0 Feb 15, 2023 Provider : repository / Type : Initial releaseRevision 1.1 May 1, 2024 Group : Data collection / Refinement descriptionCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim Item : _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ... _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id Revision 2.0 Jun 17, 2026 Group : Advisory / Atomic model ... Advisory / Atomic model / Author supporting evidence / Data collection / Database references / Derived calculations / Other / Refinement description / Source and taxonomy / Structure summary Category : atom_site / atom_site_anisotrop ... atom_site / atom_site_anisotrop / cell / citation / citation_author / entity / entity_src_gen / pdbx_audit_support / pdbx_contact_author / pdbx_distant_solvent_atoms / pdbx_entity_instance_feature / pdbx_entry_details / pdbx_initial_refinement_model / pdbx_nonpoly_scheme / pdbx_refine_tls_group / pdbx_struct_assembly / pdbx_struct_special_symmetry / pdbx_validate_close_contact / refine / refine_hist / refine_ls_restr / refine_ls_restr_ncs / refine_ls_shell / reflns / struct_ncs_dom / struct_ncs_dom_lim Item : _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] ... _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][3] / _cell.angle_beta / _cell.length_a / _cell.length_b / _cell.length_c / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _entity.src_method / _entity_src_gen.gene_src_strain / _entity_src_gen.pdbx_gene_src_scientific_name / _pdbx_audit_support.country / _pdbx_distant_solvent_atoms.auth_seq_id / _pdbx_entry_details.has_protein_modification / _pdbx_initial_refinement_model.accession_code / _pdbx_initial_refinement_model.source_name / _pdbx_initial_refinement_model.type / _pdbx_nonpoly_scheme.asym_id / _pdbx_nonpoly_scheme.auth_seq_num / _pdbx_nonpoly_scheme.ndb_seq_num / _pdbx_nonpoly_scheme.pdb_seq_num / _pdbx_nonpoly_scheme.pdb_strand_id / _pdbx_refine_tls_group.beg_auth_asym_id / _pdbx_refine_tls_group.beg_auth_seq_id / _pdbx_refine_tls_group.end_auth_asym_id / _pdbx_refine_tls_group.end_auth_seq_id / _pdbx_struct_assembly.details / _pdbx_struct_special_symmetry.auth_seq_id / _refine.B_iso_max / _refine.B_iso_mean / _refine.B_iso_min / _refine.details / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_obs / _refine.ls_d_res_high / _refine_hist.cycle_id / _refine_hist.d_res_high / _refine_hist.number_atoms_total / _refine_hist.pdbx_B_iso_mean_ligand / _refine_hist.pdbx_B_iso_mean_solvent / _refine_hist.pdbx_number_atoms_ligand / _refine_hist.pdbx_number_atoms_protein / _refine_hist.pdbx_number_residues_total / _refine_ls_restr.dev_ideal / _refine_ls_restr.number / _refine_ls_restr.type / _refine_ls_shell.R_factor_R_free_error / _refine_ls_shell.d_res_high / _reflns.d_resolution_high Provider : author / Type : Coordinate replacement
Show all Show less