9FDK
Crystal Structure of oxidized NuoEF variant R66G(NuoF) from Aquifex aeolicus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003954 | molecular_function | NADH dehydrogenase 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 | 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 | 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 | 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 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 |