Entry Database : PDB / ID : 5wi3 Structure visualization Downloads & linksTitle Structure of Acinetobacter baumannii carbapenemase OXA-239 K82D bound to cefotaxime ComponentsOXA-239 Details Keywords HYDROLASE / beta-lactamase / antibiotic resistanceFunction / homology Function and homology informationFunction Domain/homology Component
Penicillin-binding protein, transpeptidase / Penicillin binding protein transpeptidase domain / Beta-lactamase / DD-peptidase/beta-lactamase superfamily / Beta-lactamase/transpeptidase-like / Prokaryotic membrane lipoprotein lipid attachment site profile. / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homologyBiological species Acinetobacter sp. enrichment culture clone 8407 (environmental samples)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.81 Å DetailsAuthors Harper, T.M. / June, C.M. / Powers, R.A. / Leonard, D.A. Funding support United States, 2items Details Hide detailsOrganization Grant number Country National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) 1R15AI082416 United States National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) R15AI094489 United States
CitationJournal : Biochem. J. / Year : 2018Title : Multiple substitutions lead to increased loop flexibility and expanded specificity in Acinetobacter baumannii carbapenemase OXA-239.Authors : Harper, T.M. / June, C.M. / Taracila, M.A. / Bonomo, R.A. / Powers, R.A. / Leonard, D.A. History Deposition Jul 18, 2017 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Dec 27, 2017 Provider : repository / Type : Initial releaseRevision 1.1 Jan 24, 2018 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 Sep 19, 2018 Group : Atomic model / Data collection ... Atomic model / Data collection / Derived calculations / Non-polymer description / Source and taxonomy / Structure summary Category : atom_site / chem_comp ... atom_site / chem_comp / entity / entity_src_gen / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / struct_conn / struct_site 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_atom_id / _atom_site.auth_comp_id / _atom_site.label_atom_id / _atom_site.label_comp_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.pdbx_synonyms / _chem_comp.type / _entity.pdbx_description / _entity_src_gen.pdbx_host_org_strain / _pdbx_entity_nonpoly.comp_id / _pdbx_entity_nonpoly.name / _pdbx_nonpoly_scheme.mon_id / _pdbx_nonpoly_scheme.pdb_mon_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_site.details / _struct_site.pdbx_auth_comp_id Revision 2.1 Dec 11, 2019 Group : Author supporting evidence / Category : pdbx_audit_support / Item : _pdbx_audit_support.funding_organizationRevision 2.2 Oct 4, 2023 Group : Data collection / Database references / Refinement descriptionCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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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