Entry Database : PDB / ID : 5ve4 Structure visualization Downloads & linksTitle Crystal structure of persulfide dioxygenase-rhodanese fusion protein with rhodanese domain inactivating mutation (C314S) from Burkholderia phytofirmans ComponentsBpPRF Details Keywords OXIDOREDUCTASE / TRANSFERASE / persulfide dioxygenase / rhodaneseFunction / homology Function and homology informationFunction Domain/homology Component
hydrogen sulfide metabolic process / sulfur dioxygenase activity / glutathione metabolic process / metal ion binding Similarity search - Function Persulfide dioxygenase-like, MBL-fold metallo-hydrolase domain / Rhodanese-like domain / Oxidized Rhodanese; domain 1 / Rhodanese Homology Domain / Rhodanese-like domain / Rhodanese domain profile. / Rhodanese-like domain superfamily / Rhodanese-like domain / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase superfamily ... Persulfide dioxygenase-like, MBL-fold metallo-hydrolase domain / Rhodanese-like domain / Oxidized Rhodanese; domain 1 / Rhodanese Homology Domain / Rhodanese-like domain / Rhodanese domain profile. / Rhodanese-like domain superfamily / Rhodanese-like domain / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase / Ribonuclease Z/Hydroxyacylglutathione hydrolase-like / Metallo-beta-lactamase; Chain A / Ribonuclease Z/Hydroxyacylglutathione hydrolase-like / 4-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homologyBiological species Paraburkholderia phytofirmans (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 2.65 Å DetailsAuthors Motl, N. / Skiba, M.A. / Smith, J.L. / Banerjee, R. Funding support United States, 2items Details Hide detailsOrganization Grant number Country National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) GM112455 United States National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) T32GM008353 United States
CitationJournal : J. Biol. Chem. / Year : 2017Title : Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase-rhodanese fusion protein functions in sulfur assimilation.Authors : Motl, N. / Skiba, M.A. / Kabil, O. / Smith, J.L. / Banerjee, R. History Deposition Apr 3, 2017 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Jul 19, 2017 Provider : repository / Type : Initial releaseRevision 1.1 Sep 6, 2017 Group : Author supporting evidence / Database references / Category : citation / pdbx_audit_supportItem : _citation.journal_volume / _citation.page_first ... _citation.journal_volume / _citation.page_first / _citation.page_last / _pdbx_audit_support.funding_organization Revision 1.2 Jan 1, 2020 Group : Author supporting evidence / Category : pdbx_audit_support / Item : _pdbx_audit_support.funding_organizationRevision 1.3 Oct 4, 2023 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _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_asym_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_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 / _struct_ncs_dom_lim.end_label_seq_id
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