Entry Database : PDB / ID : 4waj Structure visualization Downloads & linksTitle H. influenzae beta-carbonic anhydase variant P48S/A49P ComponentsCarbonic anhydrase 2 Details Keywords LYASE / carbonic anhydrase allosteric reversionFunction / homology Function and homology informationFunction Domain/homology Component
cellular response to carbon dioxide / carbon utilization / carbonic anhydrase / carbonate dehydratase activity / cellular response to oxidative stress / zinc ion binding / cytoplasm Similarity search - Function Prokaryotic-type carbonic anhydrases signature 1. / Prokaryotic-type carbonic anhydrases signature 2. / Carbonic anhydrase, prokaryotic-like, conserved site / Beta-carbonic Anhydrase; Chain A / Carbonic anhydrase / Carbonic anhydrase / Carbonic anhydrase superfamily / Carbonic anhydrase / Carbonic anhydrase / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homologyBiological species Haemophilus influenzae (bacteria)Method X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution : 2.7 Å DetailsAuthors Rowlett, R.S. / Hoffmann, K.M. Funding support United States, 1items Details Hide detailsOrganization Grant number Country National Science Foundation (NSF, United States) MCB-1157332 United States
CitationJournal : Biochemistry / Year : 2015Title : Allosteric Reversion of Haemophilus influenzae beta-Carbonic Anhydrase via a Proline Shift.Authors : Hoffmann, K.M. / Million-Perez, H.R. / Merkhofer, R. / Nicholson, H. / Rowlett, R.S. History Deposition Aug 29, 2014 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Dec 31, 2014 Provider : repository / Type : Initial releaseRevision 1.1 Jan 14, 2015 Group : Database referencesRevision 1.2 Jan 28, 2015 Group : Database referencesRevision 1.3 Sep 13, 2017 Group : Author supporting evidence / Database references ... Author supporting evidence / Database references / Derived calculations / Other / Source and taxonomy / Structure summary Category : citation / entity_src_gen ... citation / entity_src_gen / pdbx_audit_support / pdbx_database_related / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_oper_list / struct_keywords Item : _citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag ... _citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_database_related.content_type / _pdbx_database_status.pdb_format_compatible / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_assembly_prop.type / _pdbx_struct_assembly_prop.value / _pdbx_struct_oper_list.symmetry_operation / _struct_keywords.text Revision 1.4 Nov 27, 2019 Group : Author supporting evidence / Category : pdbx_audit_support / Item : _pdbx_audit_support.funding_organizationRevision 1.5 Sep 27, 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 / refine_hist Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _refine_hist.number_atoms_solvent / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_ligand / _refine_hist.pdbx_number_atoms_nucleic_acid / _refine_hist.pdbx_number_atoms_protein
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