6Q9K
Crystal structure of reduced Aquifex aeolicus NADH-quinone oxidoreductase subunits NuoE and NuoF S96M 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 | 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 | 7 |
Details | binding site for residue FES A 201 |
Chain | Residue |
A | CYS86 |
A | VAL90 |
A | CYS91 |
A | CYS127 |
A | LEU128 |
A | ALA130 |
A | CYS131 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 202 |
Chain | Residue |
A | HOH343 |
A | LYS25 |
A | ARG27 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 203 |
Chain | Residue |
A | PHE73 |
A | ASP74 |
A | ARG75 |
A | GLU76 |
A | HOH357 |
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 | 21 |
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 | GLY394 |
B | NAI503 |
B | HOH658 |
B | HOH660 |
B | HOH679 |
B | HOH690 |
B | HOH760 |
site_id | AC6 |
Number of Residues | 24 |
Details | binding site for residue NAI B 503 |
Chain | Residue |
B | GLY67 |
B | GLY68 |
B | ALA69 |
B | PHE71 |
B | LYS76 |
B | GLU95 |
B | MET96 |
B | GLU97 |
B | TYR180 |
B | GLU185 |
B | TYR205 |
B | PRO206 |
B | FMN502 |
B | HOH624 |
B | HOH686 |
B | HOH698 |
B | HOH703 |
B | HOH712 |
B | HOH722 |
B | HOH728 |
B | HOH777 |
B | HOH806 |
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 | HOH615 |
B | HOH653 |
B | HOH736 |
B | HOH801 |
B | HOH824 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue GOL B 505 |
Chain | Residue |
B | GLY159 |
B | LYS160 |
B | GLU170 |
B | HOH826 |
D | LYS25 |
D | ARG27 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue GOL B 506 |
Chain | Residue |
B | ARG87 |
B | HOH611 |
B | HOH720 |
B | HOH729 |
B | HOH821 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue NA B 507 |
Chain | Residue |
B | GLU33 |
B | HOH753 |
B | HOH926 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue NA B 508 |
Chain | Residue |
B | ARG109 |
B | HOH756 |
B | HOH843 |
B | GLU108 |
site_id | AD3 |
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 | GLY129 |
C | ALA130 |
C | CYS131 |
site_id | AD4 |
Number of Residues | 1 |
Details | binding site for residue SO4 C 202 |
Chain | Residue |
C | ARG75 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue SO4 C 203 |
Chain | Residue |
C | LYS25 |
C | ARG27 |
C | HOH567 |
site_id | AD6 |
Number of Residues | 12 |
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 | GLY396 |
site_id | AD7 |
Number of Residues | 21 |
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 | GLY183 |
D | GLU184 |
D | GLU185 |
D | VAL218 |
D | ASN219 |
D | ASN220 |
D | THR223 |
D | GLY394 |
D | NAI503 |
D | HOH681 |
D | HOH697 |
D | HOH732 |
D | HOH752 |
D | HOH753 |
site_id | AD8 |
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 | PHE79 |
D | GLU95 |
D | MET96 |
D | GLU97 |
D | TYR180 |
D | GLU185 |
D | TYR205 |
D | PRO206 |
D | FMN502 |
D | HOH620 |
D | HOH626 |
D | HOH636 |
D | HOH694 |
D | HOH696 |
D | HOH709 |
D | HOH723 |
D | HOH767 |
D | HOH780 |
D | HOH810 |
site_id | AD9 |
Number of Residues | 11 |
Details | binding site for residue GOL D 504 |
Chain | Residue |
D | TYR34 |
D | ASP37 |
D | GLY38 |
D | GLY39 |
D | GLU116 |
D | PRO228 |
D | HOH700 |
D | HOH712 |
D | HOH759 |
D | HOH774 |
D | HOH778 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue SO4 D 505 |
Chain | Residue |
B | LYS25 |
B | ARG27 |
D | LYS160 |
D | HOH814 |
site_id | AE2 |
Number of Residues | 3 |
Details | binding site for residue NA D 506 |
Chain | Residue |
B | ARG354 |
D | GLU359 |
D | ASN362 |
site_id | AE3 |
Number of Residues | 4 |
Details | binding site for residue NA D 507 |
Chain | Residue |
D | PRO243 |
D | ASP310 |
D | HOH608 |
D | HOH919 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue NA D 508 |
Chain | Residue |
D | GLU108 |
D | ARG109 |
D | HOH724 |
D | HOH734 |
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 |