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 | 20 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
C | PHE4-LEU24 | |
B | ARG100-GLY122 | |
B | ALA185-GLN205 | |
B | ALA283-PHE292 | |
B | TRP357-TYR379 |
site_id | SWS_FT_FI2 |
Number of Residues | 152 |
Details | TRANSMEM: Helical => ECO:0000305 |
Chain | Residue | Details |
B | PHE9-PHE28 | |
B | ALA80-PHE99 | |
B | ILE123-LEU142 | |
B | LEU165-GLY184 | |
B | VAL206-GLY225 | |
B | PRO263-THR282 | |
B | VAL293-PRO312 | |
B | LEU337-ALA356 | |
A | PHE473-VAL487 |
site_id | SWS_FT_FI3 |
Number of Residues | 130 |
Details | TOPO_DOM: Periplasmic => ECO:0000305 |
Chain | Residue | Details |
B | ASP29-TYR79 | |
B | GLN143-LEU164 | |
B | ILE226-THR262 | |
B | PHE313-THR336 | |
A | ALA488-ARG522 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N-formylmethionine => ECO:0000269|PubMed:3281937 |
Chain | Residue | Details |
B | MET1 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | HIS186 | |
A | MET393 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N-formylmethionine => ECO:0000269|PubMed:26017780, ECO:0000269|PubMed:3281937 |
Chain | Residue | Details |
A | MET1 |