1KQG
FORMATE DEHYDROGENASE N FROM E. COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0043546 | molecular_function | molybdopterin cofactor binding |
| A | 0045333 | biological_process | cellular respiration |
| A | 0047111 | molecular_function | formate dehydrogenase (cytochrome-c-553) activity |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006788 | biological_process | heme oxidation |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009061 | biological_process | anaerobic respiration |
| B | 0009326 | cellular_component | formate dehydrogenase complex |
| B | 0015944 | biological_process | formate oxidation |
| B | 0016020 | cellular_component | membrane |
| B | 0019645 | biological_process | anaerobic electron transport chain |
| B | 0036397 | molecular_function | formate dehydrogenase (quinone) activity |
| B | 0045333 | biological_process | cellular respiration |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006788 | biological_process | heme oxidation |
| C | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0009061 | biological_process | anaerobic respiration |
| C | 0009326 | cellular_component | formate dehydrogenase complex |
| C | 0015944 | biological_process | formate oxidation |
| C | 0016020 | cellular_component | membrane |
| C | 0019645 | biological_process | anaerobic electron transport chain |
| C | 0020037 | molecular_function | heme binding |
| C | 0022904 | biological_process | respiratory electron transport chain |
| C | 0036397 | molecular_function | formate dehydrogenase (quinone) activity |
| C | 0045333 | biological_process | cellular respiration |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 A 1016 |
| Chain | Residue |
| A | CYS50 |
| A | TYR52 |
| A | CYS53 |
| A | CYS57 |
| A | CYS92 |
| A | GLY95 |
| A | VAL239 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B 805 |
| Chain | Residue |
| B | GLY41 |
| B | CYS42 |
| B | LYS43 |
| B | CYS45 |
| B | MET80 |
| B | CYS179 |
| B | ILE184 |
| B | CYS39 |
| B | ILE40 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 B 806 |
| Chain | Residue |
| B | LYS32 |
| B | CYS49 |
| B | ASN53 |
| B | THR78 |
| B | LYS97 |
| B | CYS160 |
| B | THR161 |
| B | LEU162 |
| B | CYS163 |
| B | PRO173 |
| B | CYS175 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 B 807 |
| Chain | Residue |
| B | CYS100 |
| B | MET101 |
| B | CYS103 |
| B | GLY107 |
| B | CYS108 |
| B | CYS143 |
| B | PHE145 |
| B | LYS159 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B 808 |
| Chain | Residue |
| B | CYS112 |
| B | PRO113 |
| B | SER114 |
| B | CYS133 |
| B | ILE134 |
| B | CYS136 |
| B | GLY137 |
| B | CYS139 |
| B | VAL157 |
| site_id | AC6 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE MGD A 1017 |
| Chain | Residue |
| A | TYR101 |
| A | GLN192 |
| A | VAL195 |
| A | SEC196 |
| A | LEU410 |
| A | GLN414 |
| A | HIS448 |
| A | GLY556 |
| A | PHE557 |
| A | ASN558 |
| A | SER562 |
| A | ILE582 |
| A | ASP583 |
| A | PRO584 |
| A | THR587 |
| A | SER616 |
| A | THR617 |
| A | ASP649 |
| A | THR894 |
| A | ARG896 |
| A | HIS902 |
| A | THR903 |
| A | TRP904 |
| A | ASN989 |
| A | TYR1005 |
| A | LYS1006 |
| A | MGD1018 |
| A | 6MO1019 |
| A | HOH1030 |
| A | HOH1033 |
| A | HOH1042 |
| A | HOH1144 |
| A | HOH1146 |
| A | HOH1171 |
| A | HOH1173 |
| A | HOH1263 |
| site_id | AC7 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE MGD A 1018 |
| Chain | Residue |
| A | HIS448 |
| A | THR893 |
| A | TYR895 |
| A | ARG896 |
| A | LEU897 |
| A | THR898 |
| A | HIS900 |
| A | PHE901 |
| A | HIS902 |
| A | LYS1006 |
| A | MGD1017 |
| A | 6MO1019 |
| A | HOH1032 |
| A | HOH1047 |
| A | HOH1086 |
| A | HOH1138 |
| A | LYS94 |
| A | SEC196 |
| A | GLY230 |
| A | GLY231 |
| A | ASN232 |
| A | GLU235 |
| A | ALA236 |
| A | ASP259 |
| A | PRO260 |
| A | ARG261 |
| A | THR263 |
| A | SER277 |
| A | GLY278 |
| A | ASP280 |
| A | ALA409 |
| A | LEU410 |
| A | GLY411 |
| A | HIS415 |
| A | GLY447 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 6MO A 1019 |
| Chain | Residue |
| A | SEC196 |
| A | MGD1017 |
| A | MGD1018 |
| A | HOH1053 |
| site_id | AC9 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM C 809 |
| Chain | Residue |
| B | TYR138 |
| B | TRP253 |
| C | VAL28 |
| C | ALA29 |
| C | GLY32 |
| C | PHE35 |
| C | PHE36 |
| C | ARG54 |
| C | HIS57 |
| C | PRO58 |
| C | GLY61 |
| C | LEU127 |
| C | LEU128 |
| C | GLY131 |
| C | HIS155 |
| C | HOH436 |
| C | HOH446 |
| C | HOH561 |
| site_id | BC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM C 810 |
| Chain | Residue |
| C | ARG9 |
| C | HIS18 |
| C | TRP19 |
| C | VAL21 |
| C | VAL22 |
| C | PHE25 |
| C | PHE75 |
| C | ASN79 |
| C | TYR109 |
| C | GLN113 |
| C | ILE166 |
| C | HIS169 |
| C | MET170 |
| C | ALA173 |
| C | SER179 |
| C | MET183 |
| C | HQO811 |
| C | HOH1294 |
| C | HOH1729 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE HQO C 811 |
| Chain | Residue |
| C | ASN110 |
| C | GLY112 |
| C | GLN113 |
| C | HIS169 |
| C | VAL176 |
| C | HEM810 |
| C | HOH1990 |
| site_id | BC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CDL B 812 |
| Chain | Residue |
| B | ASN15 |
| B | SER16 |
| B | PRO259 |
| B | ALA262 |
| B | ILE266 |
| B | HOH970 |
| B | HOH1059 |
| B | HOH1072 |
| B | HOH1089 |
| C | PHE25 |
| C | PHE26 |
| C | PHE37 |
| C | PRO38 |
| C | THR39 |
| C | PHE47 |
Functional Information from PROSITE/UniProt
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiGCGyCIaGCP |
| Chain | Residue | Details |
| B | CYS133-PRO144 |
| site_id | PS00551 |
| Number of Residues | 19 |
| Details | MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. NtCty.CSVgCgLlMyslgD |
| Chain | Residue | Details |
| A | ASN48-ASP66 |
| site_id | PS00932 |
| Number of Residues | 28 |
| Details | MOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AaakGInNgDrVtVsSkrGfiravAvVT |
| Chain | Residue | Details |
| A | ALA927-THR954 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 86 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:15919996 |
| Chain | Residue | Details |
| C | MET1-LYS11 | |
| C | PHE75-ASN110 | |
| C | VAL176-ILE217 | |
| A | CYS92 | |
| A | SEC196 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 92 |
| Details | TRANSMEM: Helical |
| Chain | Residue | Details |
| C | PHE12-PHE36 | |
| C | GLY53-ARG74 | |
| C | ALA111-ILE134 | |
| C | SER151-TRP175 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:15919996 |
| Chain | Residue | Details |
| C | PHE37-MET52 | |
| C | TRP135-TYR150 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| C | HIS18 | |
| B | CYS136 | |
| B | CYS139 | |
| B | CYS143 | |
| B | CYS160 | |
| B | CYS163 | |
| B | CYS175 | |
| B | CYS179 | |
| C | HIS57 | |
| C | HIS155 | |
| C | HIS169 | |
| B | CYS100 | |
| B | CYS103 | |
| B | CYS108 | |
| B | CYS112 | |
| B | CYS133 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| A | ALA188 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 563 |
| Chain | Residue | Details |
| C | HIS169 | hydrogen bond donor, proton acceptor, proton donor, single electron acceptor, single electron donor, single electron relay |
| A | HIS197 |
