7XMD
Cryo-EM structure of Cytochrome bo3 from Escherichia coli, the structure complexed with an allosteric inhibitor N4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004129 | molecular_function | cytochrome-c oxidase activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009060 | biological_process | aerobic respiration |
| A | 0009319 | cellular_component | cytochrome o ubiquinol oxidase complex |
| A | 0009486 | molecular_function | cytochrome bo3 ubiquinol oxidase activity |
| A | 0015078 | molecular_function | proton transmembrane transporter activity |
| A | 0015453 | molecular_function | oxidoreduction-driven active transmembrane transporter activity |
| A | 0015990 | biological_process | electron transport coupled proton transport |
| A | 0016020 | cellular_component | membrane |
| A | 0016682 | molecular_function | oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor |
| A | 0019646 | biological_process | aerobic electron transport chain |
| A | 0020037 | molecular_function | heme binding |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048039 | molecular_function | ubiquinone binding |
| A | 1902600 | biological_process | proton transmembrane transport |
| B | 0004129 | molecular_function | cytochrome-c oxidase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0009486 | molecular_function | cytochrome bo3 ubiquinol oxidase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016682 | molecular_function | oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor |
| B | 0022900 | biological_process | electron transport chain |
| C | 0004129 | molecular_function | cytochrome-c oxidase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0009060 | biological_process | aerobic respiration |
| C | 0009319 | cellular_component | cytochrome o ubiquinol oxidase complex |
| C | 0009486 | molecular_function | cytochrome bo3 ubiquinol oxidase activity |
| C | 0015078 | molecular_function | proton transmembrane transporter activity |
| C | 0015453 | molecular_function | oxidoreduction-driven active transmembrane transporter activity |
| C | 0015990 | biological_process | electron transport coupled proton transport |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019646 | biological_process | aerobic electron transport chain |
| C | 0022904 | biological_process | respiratory electron transport chain |
| D | 0005515 | molecular_function | protein binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0009060 | biological_process | aerobic respiration |
| D | 0009319 | cellular_component | cytochrome o ubiquinol oxidase complex |
| D | 0009486 | molecular_function | cytochrome bo3 ubiquinol oxidase activity |
| D | 0015078 | molecular_function | proton transmembrane transporter activity |
| D | 0015453 | molecular_function | oxidoreduction-driven active transmembrane transporter activity |
| D | 0015990 | biological_process | electron transport coupled proton transport |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019646 | biological_process | aerobic electron transport chain |
Functional Information from PROSITE/UniProt
| site_id | PS00077 |
| Number of Residues | 55 |
| Details | COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WAWGHPeVyililpvfgvfseiaatfsrkrlfgytslvwatvcitvlsfivwl..HH |
| Chain | Residue | Details |
| A | TRP280-HIS334 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=I"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 105 |
| Details | Topological domain: {"description":"Cytoplasmic"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 27 |
| Details | Transmembrane: {"description":"Helical; Name=II"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 77 |
| Details | Topological domain: {"description":"Periplasmic"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 36 |
| Details | Transmembrane: {"description":"Helical; Name=III"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=IV"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 30 |
| Details | Transmembrane: {"description":"Helical; Name=V"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 35 |
| Details | Transmembrane: {"description":"Helical; Name=VI"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 36 |
| Details | Transmembrane: {"description":"Helical; Name=VII"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 14 |
| Details | Transmembrane: {"description":"Helical; Name=VIII"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=IX"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 31 |
| Details | Transmembrane: {"description":"Helical; Name=X"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 32 |
| Details | Transmembrane: {"description":"Helical; Name=XI"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=XII"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 31 |
| Details | Transmembrane: {"description":"Helical; Name=XIII"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=XIV"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=XV"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33408407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34417297","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WTI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CUW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7N9Z","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"34417297","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CUW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"34417297","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CUW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7N9Z","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11017202","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33408407","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FFT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WTI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11017202","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FFT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11017202","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33408407","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FFT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WTI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33408407","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WTI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"PubMed","id":"34417297","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI28 |
| Number of Residues | 79 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI29 |
| Number of Residues | 179 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI30 |
| Number of Residues | 75 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI31 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"S-diacylglycerol cysteine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00303","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 23 |
| Details | M-CSA 714 |
| Chain | Residue | Details |
| A | TYR61 | proton shuttle (general acid/base) |
| A | THR149 | proton shuttle (general acid/base) |
| A | THR201 | proton shuttle (general acid/base) |
| A | THR204 | proton shuttle (general acid/base) |
| A | THR211 | proton shuttle (general acid/base) |
| A | HIS284 | metal ligand, modifies pKa |
| A | GLU286 | proton shuttle (general acid/base) |
| A | TYR288 | electron shuttle, proton shuttle (general acid/base) |
| A | SER299 | proton shuttle (general acid/base) |
| A | SER315 | proton shuttle (general acid/base) |
| A | THR359 | proton shuttle (general acid/base) |
| A | ARG71 | electrostatic stabiliser |
| A | LYS362 | proton shuttle (general acid/base) |
| A | HIS419 | electron shuttle |
| A | PHE420 | electron shuttle |
| A | HIS421 | electron shuttle |
| A | ASP75 | electrostatic stabiliser |
| A | MET79 | electron shuttle |
| A | PHE103 | electron shuttle |
| A | ASN124 | proton shuttle (general acid/base) |
| A | ASP135 | proton shuttle (general acid/base) |
| A | ASN142 | proton shuttle (general acid/base) |
| A | SER145 | proton shuttle (general acid/base) |
