Entry Database : PDB / ID : 4x9n Structure visualization Downloads & linksTitle Dithionite reduced L-alpha-Glycerophosphate Oxidase from Mycoplasma pneumoniae with FAD bound ComponentsL-alpha-glycerophosphate oxidase Details Keywords OXIDOREDUCTASE / flavoenzyme / oxidase / glycerol-3-phosphate oxidase / glycerol-3-phosphate dehydrogenaseFunction / homology Function and homology informationFunction Domain/homology Component
glycerol-3-phosphate oxidase / glycerol catabolic process / oxidoreductase activity / plasma membrane / cytoplasm Similarity search - Function FAD dependent oxidoreductase / FAD dependent oxidoreductase / D-Amino Acid Oxidase, subunit A, domain 2 / D-Amino Acid Oxidase; Chain A, domain 2 / FAD/NAD(P)-binding domain / FAD/NAD(P)-binding domain / 3-Layer(bba) Sandwich / FAD/NAD(P)-binding domain superfamily / Prokaryotic membrane lipoprotein lipid attachment site profile. / 2-Layer Sandwich / Alpha Beta Similarity search - Domain/homologyBiological species Mycoplasma pneumoniae (Filterable agent of primary atypical pneumonia)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 2.499 Å DetailsAuthors Elkhal, C.K. / Kean, K.M. / Parsonage, D. / Claiborne, A. / Karplus, P.A. CitationJournal : Febs J. / Year : 2015Title : Structure and proposed mechanism of l-alpha-glycerophosphate oxidase from Mycoplasma pneumoniae.Authors : Elkhal, C.K. / Kean, K.M. / Parsonage, D. / Maenpuen, S. / Chaiyen, P. / Claiborne, A. / Karplus, P.A. History Deposition Dec 11, 2014 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Mar 4, 2015 Provider : repository / Type : Initial releaseRevision 1.1 Apr 1, 2015 Group : Database referencesRevision 1.2 Sep 2, 2015 Group : Database referencesRevision 1.3 Sep 27, 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 / pdbx_struct_oper_list / struct_conn 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_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _pdbx_struct_oper_list.symmetry_operation / _struct_conn.pdbx_dist_value / _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_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_conn.ptnr2_symmetry
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