1QLE
CRYO-STRUCTURE OF THE PARACOCCUS DENITRIFICANS FOUR-SUBUNIT CYTOCHROME C OXIDASE IN THE COMPLETELY OXIDIZED STATE COMPLEXED WITH AN ANTIBODY FV FRAGMENT
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 | 0006811 | biological_process | monoatomic ion transport |
| 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 | 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 | 0005886 | cellular_component | plasma membrane |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0022900 | biological_process | electron transport chain |
| B | 0042773 | biological_process | ATP synthesis coupled electron transport |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070469 | cellular_component | respirasome |
| B | 1902600 | biological_process | proton transmembrane transport |
| C | 0004129 | molecular_function | cytochrome-c oxidase activity |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0009055 | molecular_function | electron transfer activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CU Y 2 |
| Chain | Residue |
| A | HIS276 |
| A | HIS325 |
| A | HIS326 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA Z 1 |
| Chain | Residue |
| A | GLU56 |
| A | HIS59 |
| A | PRO60 |
| A | GLY61 |
| A | GLN63 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN Z 2 |
| Chain | Residue |
| A | ASP404 |
| B | GLU218 |
| A | HIS403 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEA X 1 |
| Chain | Residue |
| A | LEU36 |
| A | ALA39 |
| A | GLY40 |
| A | VAL47 |
| A | THR50 |
| A | ARG54 |
| A | TRP87 |
| A | ILE91 |
| A | HIS94 |
| A | MET98 |
| A | VAL103 |
| A | ALA106 |
| A | GLY163 |
| A | TRP164 |
| A | TYR406 |
| A | VAL409 |
| A | PHE412 |
| A | HIS413 |
| A | MET416 |
| A | SER417 |
| A | VAL421 |
| A | MET452 |
| A | ARG473 |
| A | ARG474 |
| A | TYR475 |
| A | PHE500 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEA X 2 |
| Chain | Residue |
| A | TRP164 |
| A | VAL279 |
| A | TYR280 |
| A | HIS325 |
| A | HIS326 |
| A | ALA348 |
| A | THR351 |
| A | GLY387 |
| A | GLY390 |
| A | VAL391 |
| A | LEU393 |
| A | SER394 |
| A | ASP399 |
| A | HIS403 |
| A | VAL408 |
| A | HIS411 |
| A | PHE412 |
| A | VAL415 |
| A | ARG473 |
| A | ARG474 |
| B | VAL45 |
| B | ILE88 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CUA Y 1 |
| Chain | Residue |
| B | HIS181 |
| B | CYS216 |
| B | GLU218 |
| B | CYS220 |
| B | HIS224 |
| B | MET227 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PC1 P 2 |
| Chain | Residue |
| A | LEU233 |
| A | TRP323 |
| A | GLN336 |
| A | TYR339 |
| B | ARG198 |
| C | VAL102 |
| C | TRP106 |
| C | LYS110 |
| C | TYR114 |
| C | PRO121 |
| C | ASP124 |
| D | SER37 |
| D | ASN48 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PC1 P 3 |
| Chain | Residue |
| C | LEU55 |
| C | TRP66 |
| C | VAL69 |
| C | VAL70 |
| C | GLY73 |
| C | GLU74 |
| C | HIS78 |
| C | LEU86 |
| C | PHE90 |
| C | ILE222 |
| C | ILE225 |
| C | PHE226 |
| C | VAL229 |
| C | ARG233 |
| C | GLN238 |
| C | THR240 |
| C | GLN243 |
| C | HIS244 |
| C | VAL245 |
| C | GLY246 |
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 | 31 |
| Details | TRANSMEM: Helical |
| Chain | Residue | Details |
| D | ARG17-ASN48 | |
| C | HIS78-THR79 | |
| C | ASP167-ARG168 | |
| C | GLN238-HIS244 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | TOPO_DOM: Periplasmic |
| Chain | Residue | Details |
| D | SER49 | |
| C | TRP49-GLU77 | |
| C | PRO80-PRO115 | |
| C | LEU140-GLY166 | |
| C | LYS169-ALA197 | |
| C | VAL204-GLY237 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 39 |
| Details | TOPO_DOM: Periplasmic |
| Chain | Residue | Details |
| C | GLY37-PRO48 | |
| C | MET116-HIS139 | |
| C | PHE198-THR203 |
| 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 |
