7ARD
Cryo-EM structure of Polytomella Complex-I (complete composition)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
B | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
B | 0048038 | molecular_function | quinone binding |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
C | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
C | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
D | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
D | 0048038 | molecular_function | quinone binding |
D | 0051287 | molecular_function | NAD binding |
E | 0016491 | molecular_function | oxidoreductase activity |
F | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
F | 0010181 | molecular_function | FMN binding |
F | 0051287 | molecular_function | NAD binding |
F | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
G | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
G | 0016020 | cellular_component | membrane |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
G | 0042773 | biological_process | ATP synthesis coupled electron transport |
G | 0051536 | molecular_function | iron-sulfur cluster binding |
H | 0016020 | cellular_component | membrane |
I | 0016020 | cellular_component | membrane |
I | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
I | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
J | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
k | 0005739 | cellular_component | mitochondrion |
k | 0022900 | biological_process | electron transport chain |
K | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
K | 0042773 | biological_process | ATP synthesis coupled electron transport |
L | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
L | 0042773 | biological_process | ATP synthesis coupled electron transport |
M | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
M | 0042773 | biological_process | ATP synthesis coupled electron transport |
n | 0005739 | cellular_component | mitochondrion |
n | 0005743 | cellular_component | mitochondrial inner membrane |
n | 0006120 | biological_process | mitochondrial electron transport, NADH to ubiquinone |
o | 0005739 | cellular_component | mitochondrion |
q | 0016020 | cellular_component | membrane |
q | 0032981 | biological_process | mitochondrial respiratory chain complex I assembly |
Q | 0022900 | biological_process | electron transport chain |
T | 0006633 | biological_process | fatty acid biosynthetic process |
T | 0031177 | molecular_function | phosphopantetheine binding |
U | 0006633 | biological_process | fatty acid biosynthetic process |
V | 0022904 | biological_process | respiratory electron transport chain |
X | 0006120 | biological_process | mitochondrial electron transport, NADH to ubiquinone |
z | 0016740 | molecular_function | transferase activity |
Functional Information from PROSITE/UniProt
site_id | PS00012 |
Number of Residues | 16 |
Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. ELGLDSLDTVELVMAL |
Chain | Residue | Details |
T | GLU75-LEU90 |
site_id | PS00101 |
Number of Residues | 29 |
Details | HEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. IGnnViIsekAtVEdnTiLApgSyVpedV |
Chain | Residue | Details |
z | ILE142-VAL170 |
site_id | PS00198 |
Number of Residues | 12 |
Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiSCKlCEaICP |
Chain | Residue | Details |
I | CYS130-PRO141 | |
I | CYS169-PRO180 |
site_id | PS00535 |
Number of Residues | 12 |
Details | COMPLEX1_49K Respiratory chain NADH dehydrogenase 49 Kd subunit signature. LHRGtEKLlEyK |
Chain | Residue | Details |
D | LEU48-LYS59 |
site_id | PS00542 |
Number of Residues | 22 |
Details | COMPLEX1_30K Respiratory chain NADH dehydrogenase 30 Kd subunit signature. EREtwDMFgvffsnHpdlRrVL |
Chain | Residue | Details |
C | GLU140-LEU161 |
site_id | PS00641 |
Number of Residues | 18 |
Details | COMPLEX1_75K_1 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. PrfCYhqrlsiaGnCRmC |
Chain | Residue | Details |
G | PRO73-CYS90 |
site_id | PS00642 |
Number of Residues | 13 |
Details | COMPLEX1_75K_2 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. CPiCDqGGeCdLQ |
Chain | Residue | Details |
G | CYS140-GLN152 |
site_id | PS00643 |
Number of Residues | 11 |
Details | COMPLEX1_75K_3 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. RCIhCtRCVrF |
Chain | Residue | Details |
G | ARG187-PHE197 |
site_id | PS00644 |
Number of Residues | 16 |
Details | COMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GAGAYICGEETALIES |
Chain | Residue | Details |
F | GLY208-SER223 |
site_id | PS00645 |
Number of Residues | 12 |
Details | COMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ESCGqCtPCReG |
Chain | Residue | Details |
F | GLU385-GLY396 |
site_id | PS00667 |
Number of Residues | 16 |
Details | COMPLEX1_ND1_1 Respiratory-chain NADH dehydrogenase subunit 1 signature 1. GILQpFwDGFKLAvKE |
Chain | Residue | Details |
H | GLY43-GLU58 |
site_id | PS00668 |
Number of Residues | 14 |
Details | COMPLEX1_ND1_2 Respiratory-chain NADH dehydrogenase subunit 1 signature 2. PFDLPEAEaeLVa.G |
Chain | Residue | Details |
H | PRO193-GLY206 |
site_id | PS01099 |
Number of Residues | 19 |
Details | COMPLEX1_24K Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. DgtFTlgemeCMGaCvnAP |
Chain | Residue | Details |
E | ASP174-PRO192 |
site_id | PS01150 |
Number of Residues | 17 |
Details | COMPLEX1_20K Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. GcDRVVPVDVYvPgCPP |
Chain | Residue | Details |
B | GLY120-PRO136 |