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 | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0022900 | biological_process | electron transport chain |
| C | 0002250 | biological_process | adaptive immune response |
| C | 0002376 | biological_process | immune system process |
| C | 0003823 | molecular_function | antigen binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0016064 | biological_process | immunoglobulin mediated immune response |
| C | 0019814 | cellular_component | immunoglobulin complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU B 270 |
| Chain | Residue |
| B | CYS216 |
| B | GLU218 |
| B | CYS220 |
| B | HIS224 |
| B | CU271 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU B 271 |
| Chain | Residue |
| B | HIS181 |
| B | CYS216 |
| B | CYS220 |
| B | MET227 |
| B | CU270 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CU A 559 |
| Chain | Residue |
| A | HIS276 |
| A | HIS325 |
| A | HIS326 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 560 |
| Chain | Residue |
| A | HIS403 |
| A | ASP404 |
| A | HOH574 |
| B | SER217 |
| B | GLU218 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 561 |
| Chain | Residue |
| A | GLU56 |
| A | HIS59 |
| A | GLY61 |
| A | GLN63 |
| A | ASP477 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEA A 562 |
| Chain | Residue |
| A | THR50 |
| A | ARG54 |
| A | TRP87 |
| A | ILE91 |
| A | HIS94 |
| A | MET98 |
| A | MET99 |
| A | VAL103 |
| A | GLY163 |
| A | TRP164 |
| A | TYR406 |
| A | HIS413 |
| A | MET416 |
| A | SER417 |
| A | PHE460 |
| A | ARG473 |
| A | ARG474 |
| A | TYR475 |
| A | SER496 |
| A | PHE503 |
| A | HOH575 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEA A 563 |
| Chain | Residue |
| A | TRP164 |
| A | TRP272 |
| A | VAL279 |
| A | TYR280 |
| A | HIS325 |
| A | HIS326 |
| A | THR344 |
| A | ILE347 |
| A | ALA348 |
| A | THR351 |
| A | GLY352 |
| A | GLY387 |
| A | GLY390 |
| A | LEU393 |
| A | SER394 |
| A | ASP399 |
| A | HIS403 |
| A | VAL408 |
| A | HIS411 |
| A | PHE412 |
| A | VAL415 |
| A | MET416 |
| A | ARG473 |
| A | HOH571 |
| A | HOH572 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LDA B 272 |
| Chain | Residue |
| A | PHE465 |
| A | ARG468 |
| A | LDA569 |
| B | ASN19 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE LDA B 273 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE LDA A 564 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LDA A 565 |
| Chain | Residue |
| A | TRP363 |
| B | ASN74 |
| B | TRP81 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LDA A 566 |
| Chain | Residue |
| A | LEU511 |
| A | ILE33 |
| A | SER436 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LDA A 568 |
| Chain | Residue |
| A | TRP443 |
| A | GLY505 |
| A | ILE506 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LDA B 274 |
| Chain | Residue |
| B | VAL90 |
| B | ALA94 |
| B | PRO98 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LDA A 569 |
| Chain | Residue |
| A | PHE461 |
| B | LDA272 |
| site_id | CA |
| Number of Residues | 4 |
| Details | NON REDOX ACTIVE CA BINDING SITE. |
| Chain | Residue |
| A | GLU56 |
| A | HIS59 |
| A | GLY61 |
| A | GLN63 |
| site_id | CUA |
| Number of Residues | 6 |
| Details | CU A BINDING SITE. |
| Chain | Residue |
| B | HIS181 |
| B | CYS216 |
| B | GLU218 |
| B | CYS220 |
| B | HIS224 |
| B | MET227 |
| site_id | CUB |
| Number of Residues | 3 |
| Details | CU B BINDING SITE. |
| Chain | Residue |
| A | HIS276 |
| A | HIS325 |
| A | HIS326 |
| site_id | HM3 |
| Number of Residues | 1 |
| Details | AXIAL HEME A3 LIGAND. |
| site_id | HMA |
| Number of Residues | 2 |
| Details | AXIAL HEME A LIGANDS. |
| Chain | Residue |
| A | HIS94 |
| A | HIS413 |
| site_id | MM |
| Number of Residues | 3 |
| Details | NON REDOX ACTIVE MN/MG BINDING SITE. |
| Chain | Residue |
| A | HIS403 |
| A | ASP404 |
| B | GLU218 |
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"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 243 |
| Details | Topological domain: {"description":"Periplasmic"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 37 |
| Details | Transmembrane: {"description":"Helical; Name=II"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 38 |
| Details | Topological domain: {"description":"Cytoplasmic"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=III"} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 29 |
| Details | Transmembrane: {"description":"Helical; Name=IV"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 33 |
| Details | Transmembrane: {"description":"Helical; Name=V"} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 36 |
| Details | Transmembrane: {"description":"Helical; Name=VI"} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 27 |
| Details | Transmembrane: {"description":"Helical; Name=VII"} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 31 |
| Details | Transmembrane: {"description":"Helical; Name=VIII"} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=IX"} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 32 |
| Details | Transmembrane: {"description":"Helical; Name=X"} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=XI"} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 35 |
| Details | Transmembrane: {"description":"Helical; Name=XII"} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"axial binding residue"} |
| site_id | SWS_FT_FI16 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)"} |
| site_id | SWS_FT_FI18 |
| Number of Residues | 62 |
| Details | Transmembrane: {"description":"Helical"} |
| site_id | SWS_FT_FI19 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"PubMed","id":"2820725","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI20 |
| Number of Residues | 51 |
| Details | Region: {"description":"Framework-1"} |
| site_id | SWS_FT_FI21 |
| Number of Residues | 14 |
| Details | Region: {"description":"Complementarity-determining-1"} |
| site_id | SWS_FT_FI22 |
| Number of Residues | 27 |
| Details | Region: {"description":"Framework-2"} |
| site_id | SWS_FT_FI23 |
| Number of Residues | 22 |
| Details | Region: {"description":"Complementarity-determining-2"} |
| site_id | SWS_FT_FI24 |
| Number of Residues | 62 |
| Details | Region: {"description":"Framework-3"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 9788998 |
| Chain | Residue | Details |
| A | GLU278 | |
| A | LYS354 | |
