7ATN
Cytochrome c oxidase structure in R-state
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004129 | molecular_function | cytochrome-c oxidase activity |
A | 0005886 | cellular_component | plasma membrane |
A | 0006119 | biological_process | oxidative phosphorylation |
A | 0009060 | biological_process | aerobic respiration |
A | 0015990 | biological_process | electron transport coupled proton transport |
A | 0016020 | cellular_component | membrane |
A | 0020037 | molecular_function | heme binding |
A | 0022904 | biological_process | respiratory electron transport chain |
A | 0045277 | cellular_component | respiratory chain complex IV |
A | 0046872 | molecular_function | metal ion binding |
A | 0070469 | cellular_component | respirasome |
A | 1902600 | biological_process | proton transmembrane transport |
B | 0004129 | molecular_function | cytochrome-c oxidase activity |
B | 0005507 | molecular_function | copper ion binding |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0022900 | biological_process | electron transport chain |
C | 0004129 | molecular_function | cytochrome-c oxidase activity |
C | 0005886 | cellular_component | plasma membrane |
C | 0009055 | molecular_function | electron transfer activity |
C | 0009060 | biological_process | aerobic respiration |
C | 0016020 | cellular_component | membrane |
C | 0019646 | biological_process | aerobic electron transport chain |
C | 0022904 | biological_process | respiratory electron transport chain |
C | 1902600 | biological_process | proton transmembrane transport |
D | 0004129 | molecular_function | cytochrome-c oxidase activity |
D | 0005886 | cellular_component | plasma membrane |
D | 1902600 | biological_process | proton transmembrane transport |
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. WFFGHPeVyiiilpgfgiishvistfakkpifgylpmvlamaaigilgfvvwa..HH |
Chain | Residue | Details |
A | TRP272-HIS326 |
site_id | PS00078 |
Number of Residues | 49 |
Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHawtipafavkqdavpgriaqlwfsvdqegvyfgq......CselCginHayM |
Chain | Residue | Details |
B | VAL179-MET227 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 15 |
Details | TOPO_DOM: Cytoplasmic |
Chain | Residue | Details |
D | ALA1-ILE16 | |
C | GLU77-HIS78 | |
C | GLY166-ASP167 | |
C | GLY237-GLN243 | |
A | GLY365-PHE369 | |
A | ARG438-TYR440 | |
A | LYS515-HIS558 |
site_id | SWS_FT_FI2 |
Number of Residues | 31 |
Details | TRANSMEM: Helical |
Chain | Residue | Details |
D | ARG17-ASN48 | |
C | PRO48-GLY76 | |
C | THR79-TYR114 | |
C | HIS139-GLU165 | |
C | ARG168-ALA196 | |
C | THR203-LYS236 | |
C | HIS244-ARG273 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | TOPO_DOM: Periplasmic |
Chain | Residue | Details |
D | SER49 | |
C | PRO115-TRP138 | |
C | ALA197-ASP202 | |
A | MET332 | |
A | ALA396-ASP404 | |
A | GLY470-TYR478 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
B | HIS181 | |
B | CYS216 | |
B | GLU218 | |
B | CYS220 | |
B | HIS224 | |
B | MET227 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:2820725 |
Chain | Residue | Details |
B | GLN1 |
site_id | SWS_FT_FI6 |
Number of Residues | 29 |
Details | TRANSMEM: Helical; Name=IV |
Chain | Residue | Details |
A | TYR177-ASN206 |
site_id | SWS_FT_FI7 |
Number of Residues | 33 |
Details | TRANSMEM: Helical; Name=V |
Chain | Residue | Details |
A | PRO218-PHE251 |
site_id | SWS_FT_FI8 |
Number of Residues | 36 |
Details | TRANSMEM: Helical; Name=VI |
Chain | Residue | Details |
A | ASP263-LYS299 |
site_id | SWS_FT_FI9 |
Number of Residues | 27 |
Details | TRANSMEM: Helical; Name=VII |
Chain | Residue | Details |
A | GLY304-GLY331 |
site_id | SWS_FT_FI10 |
Number of Residues | 31 |
Details | TRANSMEM: Helical; Name=VIII |
Chain | Residue | Details |
A | SER333-GLY364 |
site_id | SWS_FT_FI11 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=IX |
Chain | Residue | Details |
A | LYS370-GLN395 |
site_id | SWS_FT_FI12 |
Number of Residues | 32 |
Details | TRANSMEM: Helical; Name=X |
Chain | Residue | Details |
A | THR405-GLY437 |
site_id | SWS_FT_FI13 |
Number of Residues | 28 |
Details | TRANSMEM: Helical; Name=XI |
Chain | Residue | Details |
A | PRO441-GLN469 |
site_id | SWS_FT_FI14 |
Number of Residues | 35 |
Details | TRANSMEM: Helical; Name=XII |
Chain | Residue | Details |
A | PRO479-GLY514 |
site_id | SWS_FT_FI15 |
Number of Residues | 3 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | HIS94 | |
A | HIS411 | |
A | HIS413 |
site_id | SWS_FT_FI16 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS276 | |
A | TYR280 | |
A | HIS325 | |
A | HIS326 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | CROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr) |
Chain | Residue | Details |
A | HIS276 | |
A | TYR280 |