Entry Database : PDB / ID : 5lp4 Structure visualization Downloads & linksTitle Penicillin-Binding Protein (PBP2) from Helicobacter pylori ComponentsPenicillin-binding protein 2 (Pbp2) Details Keywords HYDROLASE/ANTIBIOTIC / TRANSFERASE / CELL WALL / HYDROLASE-ANTIBIOTIC complexFunction / homology Function and homology informationFunction Domain/homology Component
peptidoglycan L,D-transpeptidase activity / serine-type D-Ala-D-Ala carboxypeptidase activity / penicillin binding / peptidoglycan biosynthetic process / cell wall organization / membrane Similarity search - Function Penicillin-binding protein 2 / Penicillin-binding protein, dimerisation domain / Penicillin-binding Protein dimerisation domain / Penicillin-binding protein, dimerisation domain superfamily / Penicillin-binding protein, transpeptidase / Penicillin binding protein transpeptidase domain / Beta-lactamase/transpeptidase-like Similarity search - Domain/homologyBiological species Helicobacter pylori (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 3.03 Å DetailsAuthors Contreras-Martel, C. / Martins, A. / Ecobichon, C. / Maragno, D.M. / Mattei, P.J. / El Ghachi, M. / Boneca, I.G. / Dessen, A. Funding support France, Brazil, 3items Details Hide detailsOrganization Grant number Country French National Research Agency 13-BSV8-0015-01 France FAPESP 11/52067-6 Brazil European Research Council 202283 France
CitationJournal : Nat Commun / Year : 2017Title : Molecular architecture of the PBP2-MreC core bacterial cell wall synthesis complex.Authors : Contreras-Martel, C. / Martins, A. / Ecobichon, C. / Trindade, D.M. / Mattei, P.J. / Hicham, S. / Hardouin, P. / Ghachi, M.E. / Boneca, I.G. / Dessen, A. History Deposition Aug 11, 2016 Deposition site : PDBE / Processing site : PDBERevision 1.0 Aug 23, 2017 Provider : repository / Type : Initial releaseRevision 1.1 Aug 30, 2017 Group : Database references / Structure summary / Category : citation / struct / Item : _citation.title / _struct.titleRevision 1.2 Oct 18, 2017 Group : Database references / Category : citation / citation_authorItem : _citation.country / _citation.journal_abbrev ... _citation.country / _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 Revision 1.3 Jan 24, 2018 Group : Source and taxonomy / Category : entity_src_genItem : _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strainRevision 1.4 Jan 10, 2024 Group : Author supporting evidence / Data collection ... Author supporting evidence / Data collection / Database references / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_audit_support / 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 / _pdbx_audit_support.funding_organization / _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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