Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC A 132 |
| Chain | Residue |
| A | GLN10 |
| A | LEU54 |
| A | GLN55 |
| A | GLY56 |
| A | GLY67 |
| A | VAL68 |
| A | MET69 |
| A | SER70 |
| A | PHE72 |
| A | ARG125 |
| B | ALA87 |
| A | CYS11 |
| A | CYS14 |
| A | HIS15 |
| A | ALA25 |
| A | PHE26 |
| A | PRO27 |
| A | HIS32 |
| A | TYR45 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CUA B 169 |
| Chain | Residue |
| B | HIS114 |
| B | CYS149 |
| B | GLN151 |
| B | TYR152 |
| B | CYS153 |
| B | HIS157 |
| B | MET160 |
Functional Information from PROSITE/UniProt
| 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 | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | HIS114 | |
| B | CYS149 | |
| B | CYS153 | |
| B | HIS157 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | HIS15 | |
| A | MET69 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ehk |
| Chain | Residue | Details |
| B | PHE86 | |
| B | PHE88 | |
