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 | PEO604 |
site_id | AC2 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE HEM A 602 |
Chain | Residue |
A | TYR65 |
A | LEU69 |
A | HIS72 |
A | ASN76 |
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 | HOH736 |
A | HOH744 |
A | HOH747 |
A | LEU32 |
A | GLY39 |
A | GLN42 |
A | ALA43 |
A | TYR46 |
site_id | AC3 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE HAS A 603 |
Chain | Residue |
A | TYR133 |
A | TRP229 |
A | VAL236 |
A | TYR237 |
A | HIS282 |
A | HIS283 |
A | SER309 |
A | LEU310 |
A | ALA313 |
A | ALA317 |
A | VAL350 |
A | LEU353 |
A | LEU354 |
A | PHE356 |
A | GLY360 |
A | GLY363 |
A | ASN366 |
A | ALA367 |
A | ASP372 |
A | HIS376 |
A | HIS384 |
A | PHE385 |
A | GLN388 |
A | ARG449 |
A | PEO604 |
A | HOH701 |
A | HOH812 |
A | HOH813 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEO A 604 |
Chain | Residue |
A | HIS233 |
A | VAL236 |
A | HIS283 |
A | CU601 |
A | HAS603 |
A | HOH734 |
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 | OLC613 |
A | OLC614 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE OLC A 606 |
Chain | Residue |
A | ILE115 |
A | PHE213 |
A | LEU215 |
A | TRP341 |
A | VAL347 |
A | TRP426 |
A | OLC612 |
A | OLC613 |
A | OLC614 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE OLC A 607 |
Chain | Residue |
A | THR293 |
A | ILE297 |
A | PHE304 |
A | HOH712 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE OLC A 608 |
Chain | Residue |
A | TRP143 |
A | SER212 |
A | LEU430 |
A | OLC615 |
A | HOH707 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE OLC A 609 |
Chain | Residue |
A | TRP111 |
A | OLC612 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE OLC A 610 |
Chain | Residue |
A | TYR161 |
A | LEU164 |
A | ARG168 |
A | OLC611 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE OLC A 611 |
Chain | Residue |
A | TRP167 |
A | ARG168 |
A | GLY528 |
A | OLC610 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE OLC A 612 |
Chain | Residue |
A | OLC606 |
A | OLC609 |
A | OLC613 |
A | GLY104 |
A | LEU108 |
A | PHE469 |
site_id | BC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE OLC A 613 |
Chain | Residue |
A | ASN102 |
A | LEU105 |
A | LEU108 |
A | MET112 |
A | LEU209 |
A | LEU472 |
A | OLC605 |
A | OLC606 |
A | OLC612 |
A | OLC614 |
A | HOH715 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE OLC A 614 |
Chain | Residue |
A | ARG419 |
A | OLC605 |
A | OLC606 |
A | OLC613 |
A | HOH702 |
A | HOH704 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE OLC A 615 |
Chain | Residue |
A | ARG337 |
A | TRP341 |
A | OLC608 |
A | HOH808 |
site_id | BC7 |
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 | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE OLC B 202 |
Chain | Residue |
B | PHE21 |
B | LEU32 |
B | TYR35 |
B | OLC204 |
B | HOH306 |
C | PHE31 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE OLC B 203 |
Chain | Residue |
A | TRP441 |
A | HOH713 |
A | HOH714 |
B | ARG141 |
B | GLU144 |
B | TYR145 |
C | OLC101 |
C | OLC102 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE OLC B 204 |
Chain | Residue |
B | ALA13 |
B | GLY17 |
B | PHE21 |
B | OLC202 |
site_id | CC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE OLC C 101 |
Chain | Residue |
A | PRO358 |
A | HIS440 |
B | OLC203 |
C | PHE22 |
C | GLY25 |
C | VAL29 |
C | OLC102 |
site_id | CC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE OLC C 102 |
Chain | Residue |
B | OLC203 |
C | THR18 |
C | OLC101 |
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. WWTVHPiVyfwllpayaiiytilpkqaggklvsdpmarlafllflllstpvgf..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 |