Entry Database : PDB / ID : 4pae Structure visualization Downloads & linksTitle Crystal structure of catalase-peroxidase (KatG) W78F mutant from Synechococcus elongatus PCC7942 ComponentsCatalase-peroxidase Details Keywords OXIDOREDUCTASEFunction / homology Function and homology informationFunction Domain/homology Component
catalase-peroxidase / catalase activity / hydrogen peroxide catabolic process / cellular response to hydrogen peroxide / heme binding / metal ion binding / cytosol Similarity search - Function Catalase-peroxidase haem / Peroxidase; domain 2 / Peroxidase, domain 2 / Peroxidase; domain 1 - #10 / Peroxidase; domain 1 / Peroxidase, active site / Peroxidases active site signature. / Plant heme peroxidase family profile. / Haem peroxidase / Peroxidase ... Catalase-peroxidase haem / Peroxidase; domain 2 / Peroxidase, domain 2 / Peroxidase; domain 1 - #10 / Peroxidase; domain 1 / Peroxidase, active site / Peroxidases active site signature. / Plant heme peroxidase family profile. / Haem peroxidase / Peroxidase / Haem peroxidase superfamily / Orthogonal Bundle / Mainly Alpha Similarity search - Domain/homologyBiological species Synechococcus elongatus (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / Resolution : 3.206 Å DetailsAuthors Kamachi, S. / Wada, K. / Tada, T. CitationJournal : Febs Lett. / Year : 2015Title : Crystal structure of the catalase-peroxidase KatG W78F mutant from Synechococcus elongatus PCC7942 in complex with the antitubercular pro-drug isoniazid.Authors : Kamachi, S. / Hirabayashi, K. / Tamoi, M. / Shigeoka, S. / Tada, T. / Wada, K. History Deposition Apr 8, 2014 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Jan 14, 2015 Provider : repository / Type : Initial releaseRevision 1.1 Nov 1, 2017 Group : Author supporting evidence / Data collection ... Author supporting evidence / Data collection / Database references / Derived calculations / Other / Source and taxonomy Category : citation / diffrn_source ... citation / diffrn_source / entity_src_gen / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_assembly_auth_evidence / pdbx_struct_assembly_prop / pdbx_struct_conn_angle / pdbx_struct_oper_list Item : _citation.journal_id_CSD / _diffrn_source.pdbx_synchrotron_site ... _citation.journal_id_CSD / _diffrn_source.pdbx_synchrotron_site / _entity_src_gen.pdbx_alt_source_flag / _pdbx_database_status.pdb_format_compatible / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_prop.type / _pdbx_struct_assembly_prop.value / _pdbx_struct_oper_list.symmetry_operation Revision 1.2 Dec 27, 2023 Group : Data collection / Database references / Refinement descriptionCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_validate_chiral / refine_hist Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _refine_hist.d_res_high / _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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