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 | 0022904 | biological_process | respiratory electron transport chain |
| A | 0045277 | cellular_component | respiratory chain complex IV |
| A | 0046872 | molecular_function | metal ion binding |
| 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 | 0022904 | biological_process | respiratory electron transport chain |
| B | 0042773 | biological_process | ATP synthesis coupled electron transport |
| B | 0046872 | molecular_function | metal ion binding |
| 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 | 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 |
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 | 30 |
| Details | Transmembrane: {"description":"Helical; Name=I"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 283 |
| Details | Topological domain: {"description":"Periplasmic"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 37 |
| Details | Transmembrane: {"description":"Helical; Name=II"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 59 |
| Details | Topological domain: {"description":"Cytoplasmic"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=III"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 29 |
| Details | Transmembrane: {"description":"Helical; Name=IV"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 33 |
| Details | Transmembrane: {"description":"Helical; Name=V"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 36 |
| Details | Transmembrane: {"description":"Helical; Name=VI"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 27 |
| Details | Transmembrane: {"description":"Helical; Name=VII"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 31 |
| Details | Transmembrane: {"description":"Helical; Name=VIII"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=IX"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 32 |
| Details | Transmembrane: {"description":"Helical; Name=X"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=XI"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 35 |
| Details | Transmembrane: {"description":"Helical; Name=XII"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 292 |
| Details | Transmembrane: {"description":"Helical"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"PubMed","id":"2820725","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1ar1 |
| Chain | Residue | Details |
| A | ARG473 | |
| A | TYR280 | |
| A | HIS411 | |
| A | HIS276 | |
| A | ARG474 | |
| A | PHE412 | |
| A | HIS413 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ar1 |
| Chain | Residue | Details |
| A | GLU278 | |
| A | LYS354 |
