6RX4
THE STRUCTURE OF BD OXIDASE FROM ESCHERICHIA COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006119 | biological_process | oxidative phosphorylation |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016679 | molecular_function | oxidoreductase activity, acting on diphenols and related substances as donors |
| 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 | 0046872 | molecular_function | metal ion binding |
| A | 0070069 | cellular_component | cytochrome complex |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006119 | biological_process | oxidative phosphorylation |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016682 | molecular_function | oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor |
| B | 0019646 | biological_process | aerobic electron transport chain |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070069 | cellular_component | cytochrome complex |
| C | 0005515 | molecular_function | protein binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006119 | biological_process | oxidative phosphorylation |
| C | 0016020 | cellular_component | membrane |
| C | 0016679 | molecular_function | oxidoreductase activity, acting on diphenols and related substances as donors |
| C | 0019646 | biological_process | aerobic electron transport chain |
| C | 0019867 | cellular_component | outer membrane |
| C | 0070069 | cellular_component | cytochrome complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue HEB A 601 |
| Chain | Residue |
| A | GLN152 |
| A | MET393 |
| A | GLY397 |
| A | PRO433 |
| A | ALA436 |
| A | VAL437 |
| A | GLY440 |
| A | TRP441 |
| A | ALA444 |
| A | LYS183 |
| A | HIS186 |
| A | SER190 |
| A | VAL234 |
| A | GLY238 |
| A | SER241 |
| A | MET245 |
| A | LYS252 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue HEB A 602 |
| Chain | Residue |
| A | ARG9 |
| A | PHE12 |
| A | ALA13 |
| A | ALA16 |
| A | PHE20 |
| A | PHE77 |
| A | PHE92 |
| A | ILE144 |
| A | MET151 |
| A | TRP441 |
| A | GLU445 |
| A | ARG448 |
| A | GLN449 |
| A | THR459 |
| A | HDD603 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | binding site for residue HDD A 603 |
| Chain | Residue |
| A | HIS19 |
| A | VAL23 |
| A | THR26 |
| A | PHE63 |
| A | VAL67 |
| A | GLY70 |
| A | MET73 |
| A | GLU74 |
| A | PHE104 |
| A | GLU107 |
| A | SER108 |
| A | SER140 |
| A | ALA141 |
| A | ILE144 |
| A | LEU145 |
| A | HEB602 |
| B | VAL62 |
| B | ILE65 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue PEE B 701 |
| Chain | Residue |
| B | MET190 |
| B | ARG191 |
| B | ALA289 |
| B | PHE292 |
| B | SER296 |
| B | TYR359 |
| B | PHE363 |
| B | ARG365 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue UQ8 B 702 |
| Chain | Residue |
| B | TRP12 |
| B | GLY16 |
| B | LEU19 |
| B | PHE22 |
| B | ALA82 |
| B | ILE134 |
| B | PHE138 |
| B | LEU142 |
| B | PHE215 |
| B | GLY219 |
| B | VAL222 |
| B | PHE259 |
| B | PRO269 |
| B | ILE303 |
| B | THR305 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 297 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 141 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 225 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"3281937","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
