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 | 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 | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 601 |
| Chain | Residue |
| A | HIS233 |
| A | HIS282 |
| A | HIS283 |
| A | PER604 |
| site_id | AC2 |
| Number of Residues | 28 |
| 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 | TRP133 |
| A | PHE385 |
| A | HIS386 |
| A | VAL389 |
| A | ALA390 |
| A | THR394 |
| A | TRP428 |
| A | MET432 |
| A | MET435 |
| A | ARG449 |
| A | ARG450 |
| A | ALA451 |
| A | HOH707 |
| A | HOH709 |
| A | HOH727 |
| A | LEU32 |
| A | SER36 |
| A | GLY39 |
| A | PRO40 |
| A | GLN42 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE HAS A 603 |
| Chain | Residue |
| A | TRP133 |
| A | VAL236 |
| A | TYR237 |
| A | HIS282 |
| A | HIS283 |
| A | THR302 |
| A | SER309 |
| A | LEU310 |
| A | LEU353 |
| A | PHE356 |
| A | GLY360 |
| A | GLY363 |
| A | ASN366 |
| A | ALA367 |
| A | ASP372 |
| A | HIS376 |
| A | VAL381 |
| A | HIS384 |
| A | PHE385 |
| A | GLN388 |
| A | ARG449 |
| A | PER604 |
| A | HOH701 |
| A | HOH718 |
| A | HOH730 |
| A | HOH734 |
| C | VAL11 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PER A 604 |
| Chain | Residue |
| A | HIS233 |
| A | VAL236 |
| A | HIS283 |
| A | CU601 |
| A | HAS603 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE OLC A 605 |
| Chain | Residue |
| A | TYR161 |
| A | OLC612 |
| A | OLC613 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE OLC A 606 |
| Chain | Residue |
| A | PHE213 |
| A | LEU215 |
| A | TRP341 |
| A | LEU422 |
| A | TRP426 |
| A | OLC607 |
| A | OLC611 |
| A | OLC612 |
| A | OLC613 |
| A | HOH706 |
| A | HOH713 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OLC A 607 |
| Chain | Residue |
| A | TRP143 |
| A | SER212 |
| A | PHE213 |
| A | LEU430 |
| A | OLC606 |
| A | OLC614 |
| A | HOH713 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE OLC A 608 |
| Chain | Residue |
| A | TRP111 |
| A | VAL465 |
| A | OLC611 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OLC A 609 |
| Chain | Residue |
| A | TYR161 |
| A | LEU164 |
| A | ASP165 |
| A | ARG168 |
| A | OLC610 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OLC A 610 |
| Chain | Residue |
| A | TRP167 |
| A | ARG168 |
| A | LYS171 |
| A | GLY528 |
| A | OLC609 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OLC A 611 |
| Chain | Residue |
| A | LEU108 |
| A | VAL468 |
| A | OLC606 |
| A | OLC608 |
| A | OLC612 |
| A | GLY104 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OLC A 612 |
| Chain | Residue |
| A | ASN102 |
| A | VAL151 |
| A | OLC605 |
| A | OLC606 |
| A | OLC611 |
| A | OLC613 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OLC A 613 |
| Chain | Residue |
| A | VAL205 |
| A | LEU209 |
| A | ASP415 |
| A | ARG419 |
| A | OLC605 |
| A | OLC606 |
| A | OLC612 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC A 614 |
| Chain | Residue |
| A | ARG337 |
| A | TRP341 |
| A | LEU430 |
| A | OLC607 |
| site_id | BC6 |
| 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 | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC B 202 |
| Chain | Residue |
| B | PHE21 |
| B | LEU32 |
| B | TYR35 |
| C | PHE31 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE OLC B 203 |
| Chain | Residue |
| A | TRP441 |
| A | LEU444 |
| A | HOH744 |
| B | ARG141 |
| B | GLU144 |
| B | TYR145 |
| C | ARG33 |
| C | OLC101 |
| C | OLC102 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OLC B 204 |
| Chain | Residue |
| B | TYR14 |
| B | GLY17 |
| B | PHE21 |
| B | TYR35 |
| B | HOH309 |
| B | HOH312 |
| B | HOH313 |
| C | HOH201 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE OLC B 205 |
| site_id | CC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE OLC C 101 |
| Chain | Residue |
| A | PRO358 |
| A | VAL437 |
| A | HIS440 |
| A | HOH744 |
| B | OLC203 |
| C | PHE22 |
| C | GLY25 |
| C | VAL29 |
| C | ALA32 |
| C | OLC102 |
| C | HOH202 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC C 102 |
| Chain | Residue |
| B | OLC203 |
| C | THR18 |
| C | OLC101 |
| C | HOH202 |
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. WWTGHPiVyfwllpayaiiytilpkqaggklvsdpmarlafllflllstpvgf..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 | 30 |
| Details | TRANSMEM: Helical |
| Chain | Residue | Details |
| C | LYS4-GLY34 | |
| A | PHE385-LEU405 | |
| A | LEU420-HIS440 | |
| A | VAL471-VAL491 | |
| A | ILE527-VAL547 | |
| A | VAL74-ALA94 | |
| A | LEU105-LEU125 | |
| A | ALA144-LEU164 | |
| A | VAL187-PHE207 | |
| A | LEU227-ILE247 | |
| A | LEU267-ASP287 | |
| A | VAL300-LEU320 | |
| A | ALA345-VAL365 | |
| Chain | Residue | Details |
| C | MET1 | |
| A | HIS384 | |
| A | HIS386 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 129 |
| Details | TOPO_DOM: Periplasmic |
| Chain | Residue | Details |
| B | THR39-GLU168 | |
| A | TYR237 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | HIS114 | |
| B | CYS149 | |
| B | CYS153 | |
| B | HIS157 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | CROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr) |
| Chain | Residue | Details |
| A | HIS233 | |
| A | TYR237 | |
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 |
