6HL4
wild-type NuoEF from Aquifex aeolicus - reduced form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003954 | molecular_function | NADH dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0045271 | cellular_component | respiratory chain complex I |
| A | 0045272 | cellular_component | plasma membrane respiratory chain complex I |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048038 | molecular_function | quinone binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048038 | molecular_function | quinone binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0055085 | biological_process | transmembrane transport |
| C | 0003954 | molecular_function | NADH dehydrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0045271 | cellular_component | respiratory chain complex I |
| C | 0045272 | cellular_component | plasma membrane respiratory chain complex I |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048038 | molecular_function | quinone binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| D | 0010181 | molecular_function | FMN binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0048038 | molecular_function | quinone binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0055085 | biological_process | transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue FES A 200 |
| Chain | Residue |
| A | CYS86 |
| A | SER88 |
| A | VAL90 |
| A | CYS91 |
| A | CYS127 |
| A | LEU128 |
| A | ALA130 |
| A | CYS131 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue SF4 B 501 |
| Chain | Residue |
| B | PRO199 |
| B | THR346 |
| B | CYS347 |
| B | GLY348 |
| B | GLN349 |
| B | CYS350 |
| B | CYS353 |
| B | SER391 |
| B | CYS393 |
| B | LEU395 |
| B | GLY396 |
| B | ILE181 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue FMN B 502 |
| Chain | Residue |
| B | GLY65 |
| B | ARG66 |
| B | GLY67 |
| B | LYS76 |
| B | ASN92 |
| B | ASP94 |
| B | GLU95 |
| B | TYR180 |
| B | GLY183 |
| B | GLU184 |
| B | GLU185 |
| B | VAL218 |
| B | ASN219 |
| B | ASN220 |
| B | THR223 |
| B | GLY394 |
| B | HOH616 |
| B | HOH620 |
| B | HOH630 |
| B | HOH638 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 503 |
| Chain | Residue |
| B | THR14 |
| D | LYS154 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue FES C 200 |
| Chain | Residue |
| C | CYS86 |
| C | SER88 |
| C | VAL90 |
| C | CYS91 |
| C | CYS127 |
| C | LEU128 |
| C | GLY129 |
| C | ALA130 |
| C | CYS131 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue SF4 D 500 |
| Chain | Residue |
| D | ILE181 |
| D | PRO199 |
| D | THR346 |
| D | CYS347 |
| D | GLY348 |
| D | GLN349 |
| D | CYS350 |
| D | CYS353 |
| D | SER391 |
| D | ILE392 |
| D | CYS393 |
| D | LEU395 |
| D | GLY396 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | binding site for residue FMN D 501 |
| Chain | Residue |
| D | GLY65 |
| D | ARG66 |
| D | GLY67 |
| D | LYS76 |
| D | ASN92 |
| D | ASP94 |
| D | GLU95 |
| D | TYR180 |
| D | GLY183 |
| D | GLU184 |
| D | GLU185 |
| D | VAL218 |
| D | ASN219 |
| D | ASN220 |
| D | THR223 |
| D | GLY394 |
| D | HOH603 |
| D | HOH607 |
| D | HOH618 |
| D | HOH622 |
| D | HOH630 |
Functional Information from PROSITE/UniProt
| site_id | PS01099 |
| Number of Residues | 19 |
| Details | COMPLEX1_24K Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. DgkFKivpvqCLGaCseAP |
| Chain | Residue | Details |
| A | ASP117-PRO135 |
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGFGGTGTVIvLteeddive..........AALK |
| Chain | Residue | Details |
| B | LEU314-LYS337 |
| site_id | PS00644 |
| Number of Residues | 16 |
| Details | COMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GAGAYICGEETALIES |
| Chain | Residue | Details |
| B | GLY176-SER191 |
| site_id | PS00645 |
| Number of Residues | 12 |
| Details | COMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ETCGqCtPCRvG |
| Chain | Residue | Details |
| B | GLU345-GLY356 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| B | GLY65 | |
| B | GLY176 | |
| D | GLY65 | |
| D | GLY176 | |
| C | CYS86 | |
| C | CYS91 | |
| C | CYS127 | |
| C | CYS131 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| B | CYS347 | |
| B | CYS350 | |
| B | CYS353 | |
| B | CYS393 | |
| D | CYS347 | |
| D | CYS350 | |
| D | CYS353 | |
| D | CYS393 |
