1KQF
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 | 4 |
Details | BINDING SITE FOR RESIDUE 6MO A 1016 |
Chain | Residue |
A | SEC196 |
A | MGD1018 |
A | MGD1019 |
A | HOH1052 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 A 1017 |
Chain | Residue |
A | CYS92 |
A | LYS94 |
A | GLY95 |
A | VAL239 |
A | CYS50 |
A | TYR52 |
A | CYS53 |
A | GLY56 |
A | CYS57 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 B 805 |
Chain | Residue |
B | CYS39 |
B | ILE40 |
B | GLY41 |
B | CYS42 |
B | LYS43 |
B | CYS45 |
B | MET80 |
B | CYS179 |
B | ILE184 |
site_id | AC4 |
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 | AC5 |
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 | PRO144 |
B | LYS159 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SF4 B 808 |
Chain | Residue |
B | CYS112 |
B | PRO113 |
B | SER114 |
B | ILE118 |
B | CYS133 |
B | ILE134 |
B | CYS136 |
B | GLY137 |
B | CYS139 |
B | VAL157 |
site_id | AC7 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE MGD A 1018 |
Chain | Residue |
A | TYR101 |
A | GLN192 |
A | SEC196 |
A | LEU410 |
A | GLN414 |
A | HIS448 |
A | GLY556 |
A | PHE557 |
A | ASN558 |
A | SER562 |
A | ILE582 |
A | ASP583 |
A | PRO584 |
A | LEU585 |
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 | 6MO1016 |
A | MGD1019 |
A | HOH1029 |
A | HOH1032 |
A | HOH1041 |
A | HOH1145 |
A | HOH1147 |
A | HOH1172 |
A | HOH1174 |
A | HOH1263 |
site_id | AC8 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE MGD A 1019 |
Chain | Residue |
A | GLY278 |
A | ASP280 |
A | ALA409 |
A | LEU410 |
A | GLY411 |
A | HIS415 |
A | GLY447 |
A | HIS448 |
A | THR893 |
A | TYR895 |
A | ARG896 |
A | LEU897 |
A | THR898 |
A | HIS900 |
A | PHE901 |
A | HIS902 |
A | HIS975 |
A | LYS1006 |
A | 6MO1016 |
A | MGD1018 |
A | HOH1031 |
A | HOH1046 |
A | HOH1085 |
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 |
site_id | AC9 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM C 809 |
Chain | Residue |
B | TYR138 |
B | TRP253 |
C | PHE25 |
C | VAL28 |
C | ALA29 |
C | GLY32 |
C | PHE35 |
C | PHE36 |
C | ARG54 |
C | HIS57 |
C | PRO58 |
C | GLY61 |
C | ILE62 |
C | ILE124 |
C | LEU127 |
C | LEU128 |
C | GLY131 |
C | ILE134 |
C | HIS155 |
C | ALA156 |
C | HOH436 |
C | HOH446 |
C | HOH561 |
site_id | BC1 |
Number of Residues | 17 |
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 | SER179 |
C | MET183 |
C | HOH1294 |
C | HOH1729 |
site_id | BC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CDL C 812 |
Chain | Residue |
B | ASN15 |
B | SER16 |
B | ILE17 |
B | PRO259 |
B | ALA262 |
B | ILE266 |
B | HOH960 |
C | PHE37 |
C | PRO38 |
C | THR39 |
C | PHE47 |
C | MET170 |
C | HOH1083 |
C | HOH1150 |
C | HOH1263 |
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 | 3 |
Details |
Chain | Residue | Details |
A | HIS197 | |
A | CSE196 | |
C | HIS169 |
site_id | CSA2 |
Number of Residues | 3 |
Details |
Chain | Residue | Details |
A | HIS197 | |
A | CSE196 | |
C | HIS169 |
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 |