6HLA
wild-type NuoEF from Aquifex aeolicus - reduced form bound to NADH
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 | 0046872 | molecular_function | metal ion binding |
A | 0048038 | molecular_function | quinone 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 | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
B | 1902600 | biological_process | proton transmembrane transport |
C | 0003954 | molecular_function | NADH dehydrogenase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0045271 | cellular_component | respiratory chain complex I |
C | 0046872 | molecular_function | metal ion binding |
C | 0048038 | molecular_function | quinone 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 | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
D | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
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 |
A | VAL136 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue SF4 B 501 |
Chain | Residue |
B | ILE181 |
B | PRO199 |
B | THR346 |
B | CYS347 |
B | GLY348 |
B | GLN349 |
B | CYS350 |
B | CYS353 |
B | SER391 |
B | ILE392 |
B | CYS393 |
B | LEU395 |
B | GLY396 |
site_id | AC3 |
Number of Residues | 23 |
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 | SER96 |
B | TYR180 |
B | GLY183 |
B | GLU184 |
B | GLU185 |
B | VAL218 |
B | ASN219 |
B | ASN220 |
B | THR223 |
B | GLY394 |
B | NAD503 |
B | HOH622 |
B | HOH665 |
B | HOH667 |
B | HOH688 |
B | HOH734 |
site_id | AC4 |
Number of Residues | 29 |
Details | binding site for residue NAD B 503 |
Chain | Residue |
B | GLY67 |
B | GLY68 |
B | ALA69 |
B | PHE71 |
B | LYS76 |
B | GLU95 |
B | SER96 |
B | GLU97 |
B | TYR180 |
B | GLU185 |
B | TYR205 |
B | PRO206 |
B | VAL207 |
B | THR319 |
B | FMN502 |
B | HOH611 |
B | HOH620 |
B | HOH625 |
B | HOH659 |
B | HOH670 |
B | HOH681 |
B | HOH699 |
B | HOH701 |
B | HOH707 |
B | HOH732 |
B | HOH738 |
B | HOH753 |
D | TRP235 |
D | ARG239 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue NA B 504 |
Chain | Residue |
B | ASP94 |
B | ALA179 |
B | HOH696 |
B | HOH743 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue MPO B 505 |
Chain | Residue |
B | TYR34 |
B | ASP37 |
B | GLY39 |
B | PHE229 |
B | SER232 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue FES C 200 |
Chain | Residue |
C | CYS86 |
C | SER88 |
C | VAL90 |
C | CYS91 |
C | CYS127 |
C | LEU128 |
C | ALA130 |
C | CYS131 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue SF4 D 501 |
Chain | Residue |
D | SER391 |
D | CYS393 |
D | LEU395 |
D | GLY396 |
D | ILE181 |
D | PRO199 |
D | THR346 |
D | CYS347 |
D | GLY348 |
D | GLN349 |
D | CYS350 |
D | CYS353 |
site_id | AC9 |
Number of Residues | 23 |
Details | binding site for residue FMN D 502 |
Chain | Residue |
D | GLY65 |
D | ARG66 |
D | GLY67 |
D | LYS76 |
D | ASN92 |
D | ASP94 |
D | GLU95 |
D | SER96 |
D | TYR180 |
D | GLY183 |
D | GLU184 |
D | GLU185 |
D | VAL218 |
D | ASN219 |
D | ASN220 |
D | THR223 |
D | GLY394 |
D | NAD503 |
D | HOH611 |
D | HOH629 |
D | HOH659 |
D | HOH672 |
D | HOH697 |
site_id | AD1 |
Number of Residues | 20 |
Details | binding site for residue NAD D 503 |
Chain | Residue |
D | GLY67 |
D | GLY68 |
D | ALA69 |
D | PHE71 |
D | LYS76 |
D | GLU95 |
D | SER96 |
D | GLU97 |
D | TYR180 |
D | GLU185 |
D | TYR205 |
D | PRO206 |
D | THR319 |
D | FMN502 |
D | HOH613 |
D | HOH670 |
D | HOH680 |
D | HOH696 |
D | HOH706 |
D | HOH719 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue NA D 504 |
Chain | Residue |
D | ASP94 |
D | ALA179 |
D | HOH681 |
D | HOH704 |
site_id | AD3 |
Number of Residues | 10 |
Details | binding site for residue MPO D 505 |
Chain | Residue |
D | TYR34 |
D | ASP37 |
D | GLY39 |
D | LEU113 |
D | PHE229 |
D | SER232 |
D | MET233 |
D | HOH618 |
D | HOH663 |
D | HOH714 |
Functional Information from PROSITE/UniProt
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 |
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 |
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 |