Entry Database : PDB / ID : 1kqf Structure visualization Downloads & linksTitle FORMATE DEHYDROGENASE N FROM E. COLI Components(FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, ... ) x 3 Details Keywords OXIDOREDUCTASE / SELENIUM / SELENOCYSTEINE / SECYS / MOLYBDENUM / MOLYBDOPTERIN / MPT / MOLYBDOPTERIN GUANINE DINUCLEOTIDE / MGD / IRON SULFUR CLUSTER / FE4S4 / FORMATE / DEHYDROGENASE / ANAEROBIC / INTEGRAL MEMBRANE PROTEINFunction / homology Function and homology informationFunction Domain/homology Component
formate dehydrogenase-N / formate dehydrogenase (quinone) activity / formate oxidation / formate dehydrogenase (cytochrome-c-553) activity / formate dehydrogenase complex / selenium binding / anaerobic electron transport chain / heme oxidation / formate dehydrogenase (NAD+) activity / molybdenum ion binding ... formate dehydrogenase-N / formate dehydrogenase (quinone) activity / formate oxidation / formate dehydrogenase (cytochrome-c-553) activity / formate dehydrogenase complex / selenium binding / anaerobic electron transport chain / heme oxidation / formate dehydrogenase (NAD+) activity / molybdenum ion binding / anaerobic respiration / molybdopterin cofactor binding / respiratory electron transport chain / outer membrane-bounded periplasmic space / 4 iron, 4 sulfur cluster binding / electron transfer activity / membrane => GO:0016020 / heme binding / membrane / metal ion binding / plasma membrane Similarity search - Function Single helix bin / Formate dehydrogenase iron-sulphur subunit, Proteobacteria / Formate dehydrogenase, gamma subunit / Formate dehydrogenase iron-sulphur subunit / Formate dehydrogenase, transmembrane / Formate dehydrogenase, C-terminal domain superfamily / Formate dehydrogenase N, transmembrane / Cytochrome b561, bacterial/Ni-hydrogenase / Prokaryotic cytochrome b561 / Fumarate Reductase Cytochrome B subunit ... Single helix bin / Formate dehydrogenase iron-sulphur subunit, Proteobacteria / Formate dehydrogenase, gamma subunit / Formate dehydrogenase iron-sulphur subunit / Formate dehydrogenase, transmembrane / Formate dehydrogenase, C-terminal domain superfamily / Formate dehydrogenase N, transmembrane / Cytochrome b561, bacterial/Ni-hydrogenase / Prokaryotic cytochrome b561 / Fumarate Reductase Cytochrome B subunit / Transmembrane di-heme cytochromes, Chain C / Formate dehydrogenase-N, alpha subunit / 4Fe-4S binding domain / Dimethylsulfoxide Reductase; domain 2 / Dimethylsulfoxide Reductase, domain 2 / Rossmann fold - #740 / 4Fe-4S dicluster domain / Molybdopterin oxidoreductase, molybdopterin cofactor binding site / Prokaryotic molybdopterin oxidoreductases signature 1. / Prokaryotic molybdopterin oxidoreductases signature 3. / Molybdopterin oxidoreductase, prokaryotic, conserved site / Molybdopterin oxidoreductase Fe4S4 domain / Molybdopterin oxidoreductase Fe4S4 domain / 4Fe-4S binding domain / Alpha-Beta Plaits - #20 / Molybdopterin dinucleotide-binding domain / Molydopterin dinucleotide binding domain / Barwin-like endoglucanases - #20 / Barwin-like endoglucanases / Di-haem cytochrome, transmembrane / Aspartate decarboxylase-like domain superfamily / Molybdopterin oxidoreductase, 4Fe-4S domain / Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile. / Molybdopterin oxidoreductase / Molybdopterin oxidoreductase / 4Fe-4S dicluster domain / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / Twin arginine translocation (Tat) signal profile. / Twin-arginine translocation pathway, signal sequence / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Alpha-Beta Plaits / Up-down Bundle / Beta Barrel / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta Similarity search - Domain/homology : / CARDIOLIPIN / PROTOPORPHYRIN IX CONTAINING FE / Chem-MGD / IRON/SULFUR CLUSTER / Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit / Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunit / Formate dehydrogenase, nitrate-inducible, major subunit / Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunit Similarity search - ComponentBiological species Escherichia coli (E. coli)Method X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution : 1.6 Å DetailsAuthors Jormakka, M. / Tornroth, S. / Byrne, B. / Iwata, S. CitationJournal : Science / Year : 2002Title : Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.Authors : Jormakka, M. / Tornroth, S. / Byrne, B. / Iwata, S. History Deposition Jan 5, 2002 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Mar 15, 2002 Provider : repository / Type : Initial releaseRevision 1.1 Apr 27, 2008 Group : Version format complianceRevision 1.2 Jul 13, 2011 Group : Derived calculations / Version format complianceRevision 1.3 Feb 19, 2014 Group : Atomic model / Structure summaryRevision 1.4 Aug 6, 2014 Group : Derived calculations / Structure summaryRevision 1.5 Feb 14, 2024 Group : Data collection / Database references / Derived calculationsCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / 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_struct_conn_angle.ptnr1_auth_asym_id / _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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_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_asym_id / _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_asym_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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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