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 | 0016020 | cellular_component | membrane |
| A | 0020037 | molecular_function | heme binding |
| 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 | 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 | 0006811 | biological_process | monoatomic ion transport |
| C | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CU1 A 803 |
| Chain | Residue |
| A | HIS233 |
| A | HIS282 |
| A | HIS283 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 800 |
| Chain | Residue |
| A | ASN76 |
| A | ALA77 |
| A | LEU132 |
| A | TYR133 |
| A | PHE385 |
| A | HIS386 |
| A | VAL389 |
| A | ALA390 |
| A | THR394 |
| A | MET435 |
| A | ARG449 |
| A | ARG450 |
| A | ALA451 |
| A | LEU477 |
| A | GLY39 |
| A | GLN42 |
| A | TYR46 |
| A | TYR65 |
| A | LEU69 |
| A | HIS72 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE HAS A 801 |
| Chain | Residue |
| A | TYR133 |
| A | TRP229 |
| A | VAL236 |
| A | TYR237 |
| A | TRP239 |
| A | LEU240 |
| A | HIS282 |
| A | SER309 |
| A | LEU310 |
| A | ALA313 |
| A | VAL316 |
| A | TRP335 |
| A | ILE336 |
| A | VAL350 |
| A | LEU353 |
| A | LEU354 |
| A | PHE356 |
| A | GLY360 |
| A | ASN366 |
| A | ALA367 |
| A | ASP372 |
| A | HIS376 |
| A | VAL381 |
| A | HIS384 |
| A | PHE385 |
| A | GLN388 |
| A | VAL389 |
| A | ARG449 |
| C | LEU15 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CUA B 802 |
| Chain | Residue |
| B | HIS114 |
| B | CYS149 |
| B | GLN151 |
| B | CYS153 |
| B | HIS157 |
| B | MET160 |
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. WWTGHPiVyfwllpayaiiytilpkqaggrlvsdpmarlafllflllstpvgf..HH |
| Chain | Residue | Details |
| A | TRP229-HIS283 | |
| site_id | PS00078 |
| Number of Residues | 49 |
| Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHgfhvegtninvevlpgevstvrytfkrpgeyrii......CnqyCglgHqnM |
| Chain | Residue | Details |
| B | VAL112-MET160 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 260 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)"} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 64 |
| Details | Transmembrane: {"description":"Helical"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 129 |
| Details | Topological domain: {"description":"Periplasmic"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1ehk |
| Chain | Residue | Details |
| A | HIS384 | |
| A | ARG449 | |
| A | TYR237 | |
| A | HIS386 | |
| A | PHE385 | |
| A | HIS233 | |
| A | ARG450 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ehk |
| Chain | Residue | Details |
| B | PHE86 | |
| B | PHE88 | |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 735 |
| Chain | Residue | Details |
| B | PHE86 | electron shuttle |
| B | PHE88 | electron shuttle |
| A | HIS384 | electron shuttle |
| A | PHE385 | electron shuttle |
| A | HIS386 | electron shuttle |
| A | ARG449 | electron shuttle |
| A | ARG450 | electron shuttle |
