Entry Database : PDB / ID : 2vqa Structure visualization Downloads & linksTitle Protein-folding location can regulate Mn versus Cu- or Zn-binding. Crystal Structure of MncA. ComponentsSLL1358 PROTEIN Details Keywords METAL BINDING PROTEIN / PERIPLASMIC BINDING PROTEIN / METAL-BINDING PROTEIN / MN2+ / CUPIN / BI-CUPIN / OXALATE DECARBOXYLASEFunction / homology Function and homology informationFunction Domain/homology Component
oxalate metabolic process / nutrient reservoir activity / outer membrane-bounded periplasmic space / metal ion binding Similarity search - Function Bicupin, oxalate decarboxylase/oxidase / Cupin / Cupin 1 / Cupin / RmlC-like cupin domain superfamily / Jelly Rolls / RmlC-like jelly roll fold / Jelly Rolls / Sandwich / Mainly Beta Similarity search - Domain/homologyBiological species SYNECHOCYSTIS SP. (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 2.95 Å DetailsAuthors Tottey, S. / Waldron, K.J. / Firbank, S.J. / Reale, B. / Bessant, C. / Sato, K. / Gray, J. / Banfield, M.J. / Dennison, C. / Robinson, N.J. CitationJournal : Nature / Year : 2008Title : Protein-Folding Location Can Regulate Manganese-Binding Versus Copper- or Zinc-Binding.Authors : Tottey, S. / Waldron, K.J. / Firbank, S.J. / Reale, B. / Bessant, C. / Sato, K. / Cheek, T.R. / Gray, J. / Banfield, M.J. / Dennison, C. / Robinson, N.J. History Deposition Mar 12, 2008 Deposition site : PDBE / Processing site : PDBERevision 1.0 Oct 28, 2008 Provider : repository / Type : Initial releaseRevision 1.1 May 30, 2012 Group : Database references / Derived calculations ... Database references / Derived calculations / Non-polymer description / Other / Version format compliance Revision 1.2 Dec 13, 2023 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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 / _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_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Show all Show less Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.