6Q9G
Crystal structure of reduced Aquifex aeolicus NADH-quinone oxidoreductase subunits NuoE G129D and NuoF 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 | 0022904 | biological_process | respiratory electron transport chain |
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 | 0022904 | biological_process | respiratory electron transport chain |
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 | 8 |
Details | binding site for residue FES A 201 |
Chain | Residue |
A | CYS86 |
A | VAL90 |
A | CYS91 |
A | CYS127 |
A | LEU128 |
A | ASP129 |
A | ALA130 |
A | CYS131 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 202 |
Chain | Residue |
A | ARG27 |
A | HOH310 |
A | LYS25 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 203 |
Chain | Residue |
A | PHE73 |
A | ARG75 |
A | GLU76 |
A | HOH321 |
site_id | AC4 |
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 | AC5 |
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 | GLY183 |
B | GLU184 |
B | GLU185 |
B | VAL218 |
B | ASN219 |
B | ASN220 |
B | THR223 |
B | NAI503 |
B | HOH667 |
B | HOH683 |
B | HOH691 |
B | HOH716 |
B | HOH780 |
site_id | AC6 |
Number of Residues | 26 |
Details | binding site for residue NAI 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 | FMN502 |
B | HOH635 |
B | HOH655 |
B | HOH680 |
B | HOH696 |
B | HOH713 |
B | HOH742 |
B | HOH758 |
B | HOH789 |
B | HOH796 |
B | HOH820 |
B | HOH845 |
D | TRP235 |
D | ARG239 |
site_id | AC7 |
Number of Residues | 11 |
Details | binding site for residue GOL B 504 |
Chain | Residue |
B | TYR34 |
B | ASP37 |
B | GLY38 |
B | GLY39 |
B | GLU116 |
B | PRO228 |
B | HOH642 |
B | HOH733 |
B | HOH741 |
B | HOH771 |
B | HOH795 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue NA B 505 |
Chain | Residue |
B | GLU33 |
B | HOH732 |
B | HOH868 |
B | HOH914 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue NA B 506 |
Chain | Residue |
B | GLU53 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue FES C 201 |
Chain | Residue |
C | CYS86 |
C | SER88 |
C | VAL90 |
C | CYS91 |
C | CYS127 |
C | LEU128 |
C | ASP129 |
C | ALA130 |
C | CYS131 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue SO4 C 202 |
Chain | Residue |
C | ASP74 |
C | ARG75 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue SO4 C 203 |
Chain | Residue |
C | LYS25 |
C | ARG27 |
site_id | AD4 |
Number of Residues | 13 |
Details | binding site for residue SF4 D 501 |
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 | AD5 |
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 | TYR180 |
D | ILE181 |
D | GLY183 |
D | GLU184 |
D | GLU185 |
D | VAL218 |
D | ASN219 |
D | ASN220 |
D | THR223 |
D | GLY394 |
D | NAI503 |
D | HOH683 |
D | HOH684 |
D | HOH691 |
D | HOH753 |
D | HOH768 |
site_id | AD6 |
Number of Residues | 24 |
Details | binding site for residue NAI 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 | FMN502 |
D | HOH625 |
D | HOH635 |
D | HOH637 |
D | HOH638 |
D | HOH654 |
D | HOH663 |
D | HOH669 |
D | HOH736 |
D | HOH737 |
D | HOH778 |
D | HOH787 |
site_id | AD7 |
Number of Residues | 9 |
Details | binding site for residue GOL D 504 |
Chain | Residue |
D | TYR34 |
D | ASP37 |
D | GLY39 |
D | GLU116 |
D | PRO228 |
D | HOH661 |
D | HOH701 |
D | HOH766 |
D | HOH767 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue SO4 D 505 |
Chain | Residue |
B | LYS25 |
B | ARG27 |
D | LYS160 |
D | GLU170 |
D | HOH846 |
site_id | AD9 |
Number of Residues | 3 |
Details | binding site for residue NA D 506 |
Chain | Residue |
D | PRO243 |
D | ASP310 |
D | HOH928 |
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 |
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 |