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 | 0022904 | biological_process | respiratory electron transport chain |
| 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 | 0022904 | biological_process | respiratory electron transport chain |
| 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 | 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 | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 601 |
| Chain | Residue |
| A | HIS233 |
| A | HIS282 |
| A | HIS283 |
| A | HAS603 |
| A | PER604 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM A 602 |
| Chain | Residue |
| A | ALA43 |
| A | TYR46 |
| A | TYR65 |
| A | LEU69 |
| A | HIS72 |
| A | ASN76 |
| A | ALA77 |
| A | LEU132 |
| A | TYR133 |
| A | PHE385 |
| A | HIS386 |
| A | ALA390 |
| A | THR394 |
| A | MET432 |
| A | MET435 |
| A | ARG449 |
| A | ARG450 |
| A | ALA451 |
| A | LEU477 |
| A | LEU32 |
| A | GLY39 |
| A | PRO40 |
| A | GLN42 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HAS A 603 |
| Chain | Residue |
| A | TYR133 |
| A | TRP229 |
| A | MET236 |
| A | TYR237 |
| A | TYR244 |
| A | HIS282 |
| A | HIS283 |
| A | SER309 |
| A | ALA313 |
| A | VAL350 |
| A | LEU353 |
| A | PHE356 |
| A | GLY363 |
| A | ASN366 |
| A | ALA367 |
| A | ASP372 |
| A | HIS376 |
| A | HIS384 |
| A | PHE385 |
| A | GLN388 |
| A | VAL389 |
| A | ARG449 |
| A | CU601 |
| A | PER604 |
| A | HOH701 |
| C | VAL11 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PER A 604 |
| Chain | Residue |
| A | HIS233 |
| A | MET236 |
| A | HIS283 |
| A | CU601 |
| A | HAS603 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OLC A 605 |
| Chain | Residue |
| A | LEU105 |
| A | VAL158 |
| A | TYR161 |
| A | ILE475 |
| A | VAL479 |
| A | OLC614 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OLC A 606 |
| Chain | Residue |
| A | PHE213 |
| A | LEU215 |
| A | TRP341 |
| A | TRP426 |
| A | OLC609 |
| A | OLC613 |
| A | OLC614 |
| A | OLC615 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OLC A 607 |
| Chain | Residue |
| A | TRP441 |
| A | LEU444 |
| B | TYR145 |
| B | HOH310 |
| C | ARG33 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC A 608 |
| Chain | Residue |
| A | THR293 |
| A | MET296 |
| A | ILE297 |
| B | HOH301 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OLC A 609 |
| Chain | Residue |
| A | TRP143 |
| A | SER212 |
| A | PHE213 |
| A | GLY214 |
| A | LEU430 |
| A | OLC606 |
| A | OLC616 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE OLC A 610 |
| Chain | Residue |
| A | TRP111 |
| A | VAL465 |
| A | OLC613 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OLC A 611 |
| Chain | Residue |
| A | TYR161 |
| A | ARG168 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC A 612 |
| Chain | Residue |
| A | TRP167 |
| A | ARG168 |
| A | LYS171 |
| A | GLY528 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OLC A 613 |
| Chain | Residue |
| A | LEU108 |
| A | VAL468 |
| A | OLC606 |
| A | OLC610 |
| A | OLC614 |
| A | GLY104 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OLC A 614 |
| Chain | Residue |
| A | GLY104 |
| A | LEU105 |
| A | MET112 |
| A | VAL151 |
| A | OLC605 |
| A | OLC606 |
| A | OLC613 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC A 615 |
| Chain | Residue |
| A | ASP415 |
| A | ALA416 |
| A | ARG419 |
| A | OLC606 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OLC A 616 |
| Chain | Residue |
| A | ARG337 |
| A | TRP341 |
| A | PHE429 |
| A | LEU430 |
| A | OLC609 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CUA B 201 |
| Chain | Residue |
| B | HIS114 |
| B | CYS149 |
| B | GLN151 |
| B | CYS153 |
| B | HIS157 |
| B | MET160 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC B 202 |
| Chain | Residue |
| B | PHE21 |
| B | LEU32 |
| B | TYR35 |
| B | OLC203 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OLC B 203 |
| Chain | Residue |
| B | ALA13 |
| B | TYR14 |
| B | GLY17 |
| B | TRP18 |
| B | TYR35 |
| B | OLC202 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC C 101 |
| Chain | Residue |
| C | PHE22 |
| C | GLY25 |
| C | VAL29 |
| C | OLC102 |
| site_id | CC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE OLC C 102 |
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 | 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 | 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 |
