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 | 3 |
Details | BINDING SITE FOR RESIDUE CU A 803 |
Chain | Residue |
A | HIS233 |
A | HIS282 |
A | HIS283 |
site_id | AC2 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE HEM A 800 |
Chain | Residue |
A | TYR65 |
A | LEU69 |
A | HIS72 |
A | ASN76 |
A | ALA77 |
A | LEU132 |
A | TYR133 |
A | PHE385 |
A | HIS386 |
A | VAL389 |
A | ALA390 |
A | THR394 |
A | TRP428 |
A | MET432 |
A | ARG449 |
A | ARG450 |
A | ALA451 |
A | LEU477 |
A | SER36 |
A | GLY39 |
A | PRO40 |
A | GLN42 |
A | ALA43 |
A | TYR46 |
site_id | AC3 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE HAS A 801 |
Chain | Residue |
A | TYR133 |
A | TRP229 |
A | VAL236 |
A | TYR237 |
A | TRP239 |
A | HIS282 |
A | HIS283 |
A | SER309 |
A | ALA313 |
A | ALA317 |
A | TRP335 |
A | VAL350 |
A | LEU353 |
A | LEU354 |
A | PHE356 |
A | GLY360 |
A | GLY363 |
A | ASN366 |
A | ALA367 |
A | ASP372 |
A | HIS376 |
A | VAL381 |
A | HIS384 |
A | PHE385 |
A | GLN388 |
A | VAL389 |
A | ARG449 |
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 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE XE A 563 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE XE A 567 |
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 | |
site_id | SWS_FT_FI2 |
Number of Residues | 129 |
Details | TOPO_DOM: Periplasmic |
Chain | Residue | Details |
B | THR39-GLU168 | |
A | HIS384 | |
A | HIS386 | |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
B | HIS114 | |
B | CYS149 | |
B | CYS153 | |
B | HIS157 | |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | HIS282 | |
A | HIS283 | |
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 |