6RKO
Cryo-EM structure of the E. coli cytochrome bd-I oxidase at 2.68 A resolution
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 |
H | 0005515 | molecular_function | protein binding |
H | 0005886 | cellular_component | plasma membrane |
H | 0016020 | cellular_component | membrane |
H | 0070069 | cellular_component | cytochrome complex |
H | 0071456 | biological_process | cellular response to hypoxia |
X | 0005515 | molecular_function | protein binding |
X | 0005886 | cellular_component | plasma membrane |
X | 0006119 | biological_process | oxidative phosphorylation |
X | 0016020 | cellular_component | membrane |
X | 0016679 | molecular_function | oxidoreductase activity, acting on diphenols and related substances as donors |
X | 0019646 | biological_process | aerobic electron transport chain |
X | 0019867 | cellular_component | outer membrane |
X | 0070069 | cellular_component | cytochrome complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | binding site for residue UQ8 B 401 |
Chain | Residue |
B | TRP12 |
B | PHE215 |
B | ALA218 |
B | GLY219 |
B | MET223 |
B | PRO269 |
B | ILE302 |
B | ILE303 |
B | THR305 |
B | ALA309 |
B | VAL314 |
B | GLY16 |
B | LEU19 |
B | LEU71 |
B | VAL78 |
B | ILE134 |
B | PHE138 |
B | LEU142 |
B | SER176 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue POV B 402 |
Chain | Residue |
B | MET190 |
B | ARG191 |
B | ALA289 |
B | VAL293 |
B | TYR359 |
B | PHE363 |
B | GLY364 |
B | ARG365 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue POV B 403 |
Chain | Residue |
B | GLU5 |
B | PHE9 |
B | HIS237 |
B | TRP328 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue POV A 601 |
Chain | Residue |
A | TYR428 |
A | PRO431 |
A | TRP434 |
A | ILE435 |
A | POV602 |
H | PHE7 |
H | THR11 |
H | VAL22 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for residue POV A 602 |
Chain | Residue |
A | LEU21 |
A | PHE22 |
A | ASN62 |
A | PHE198 |
A | TRP205 |
A | LYS209 |
A | ARG211 |
A | LEU427 |
A | GLU489 |
A | PHE494 |
A | ARG498 |
A | POV601 |
H | PHE7 |
site_id | AC6 |
Number of Residues | 20 |
Details | binding site for residue HDD A 603 |
Chain | Residue |
A | HIS19 |
A | VAL23 |
A | THR26 |
A | LEU27 |
A | PHE63 |
A | GLY66 |
A | VAL67 |
A | GLY70 |
A | MET73 |
A | GLU74 |
A | PHE104 |
A | GLU107 |
A | SER108 |
A | SER140 |
A | ALA141 |
A | ILE144 |
A | HEB604 |
A | OXY606 |
A | HOH703 |
B | ILE65 |
site_id | AC7 |
Number of Residues | 18 |
Details | binding site for residue HEB A 604 |
Chain | Residue |
A | ARG9 |
A | PHE12 |
A | ALA13 |
A | ALA16 |
A | PHE77 |
A | TRP81 |
A | PHE92 |
A | ILE144 |
A | ASN148 |
A | MET151 |
A | TRP441 |
A | GLU445 |
A | TYR446 |
A | ARG448 |
A | GLN449 |
A | THR459 |
A | HDD603 |
H | ALA26 |
site_id | AC8 |
Number of Residues | 14 |
Details | binding site for residue HEB A 605 |
Chain | Residue |
A | VAL437 |
A | GLY440 |
A | TRP441 |
A | ALA444 |
A | HOH701 |
A | LYS183 |
A | HIS186 |
A | THR187 |
A | VAL234 |
A | ILE235 |
A | ASP239 |
A | LYS252 |
A | MET393 |
A | ALA436 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue OXY A 606 |
Chain | Residue |
A | GLU99 |
A | PHE104 |
A | SER140 |
A | ILE144 |
A | HDD603 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
X | PHE4-LEU24 | |
A | GLY70-LEU96 | |
A | ALA147-HIS186 | |
A | VAL236-PHE390 | |
A | PHE442-ILE472 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N-formylmethionine => ECO:0000269|PubMed:21050835 |
Chain | Residue | Details |
A | TRP55-THR69 | |
A | ALA97-PHE114 | |
A | VAL129-VAL146 | |
A | THR187-SER203 | |
A | PHE220-ILE235 | |
A | ARG391-SER407 | |
A | ARG424-TRP441 | |
A | PHE473-VAL487 | |
H | MET1 |
site_id | SWS_FT_FI3 |
Number of Residues | 95 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
A | MET36-PHE54 | |
A | PHE115-CYS128 | |
A | ALA204-SER219 | |
A | PHE408-LEU423 | |
A | ALA488-ARG522 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: axial binding residue => ECO:0000255 |
Chain | Residue | Details |
A | HIS19 |
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 |