7XK4
Cryo-EM structure of Na+-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae, state 2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006814 | biological_process | sodium ion transport |
| A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0006814 | biological_process | sodium ion transport |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016020 | cellular_component | membrane |
| B | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| B | 0022904 | biological_process | respiratory electron transport chain |
| B | 0055085 | biological_process | transmembrane transport |
| B | 1902444 | molecular_function | riboflavin binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006811 | biological_process | monoatomic ion transport |
| C | 0006814 | biological_process | sodium ion transport |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016020 | cellular_component | membrane |
| C | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006811 | biological_process | monoatomic ion transport |
| D | 0006814 | biological_process | sodium ion transport |
| D | 0016020 | cellular_component | membrane |
| D | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0006811 | biological_process | monoatomic ion transport |
| E | 0006814 | biological_process | sodium ion transport |
| E | 0009276 | cellular_component | Gram-negative-bacterium-type cell wall |
| E | 0016020 | cellular_component | membrane |
| E | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| E | 0022904 | biological_process | respiratory electron transport chain |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0006811 | biological_process | monoatomic ion transport |
| F | 0006814 | biological_process | sodium ion transport |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0016020 | cellular_component | membrane |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051536 | molecular_function | iron-sulfur cluster binding |
| F | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| F | 0071949 | molecular_function | FAD binding |
Functional Information from PROSITE/UniProt
| site_id | PS00089 |
| Number of Residues | 22 |
| Details | RIBORED_LARGE Ribonucleotide reductase large subunit signature. WlaVfpamfw.GMYNaggQAiaA |
| Chain | Residue | Details |
| B | TRP61-ALA82 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 160 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00426","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"FMN phosphoryl threonine","evidences":[{"source":"HAMAP-Rule","id":"MF_00426","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22366169","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00427","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"FMN phosphoryl threonine","evidences":[{"source":"HAMAP-Rule","id":"MF_00427","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22366169","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 100 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00428","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 120 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00429","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00430","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 94 |
| Details | Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"HAMAP-Rule","id":"MF_00430","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 140 |
| Details | Domain: {"description":"FAD-binding FR-type","evidences":[{"source":"HAMAP-Rule","id":"MF_00430","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00430","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15379571","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
