Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004129 | molecular_function | cytochrome-c oxidase activity |
A | 0005507 | molecular_function | copper ion binding |
A | 0005509 | molecular_function | calcium ion binding |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019333 | biological_process | denitrification pathway |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
A | 0050304 | molecular_function | nitrous-oxide reductase activity |
A | 1902600 | biological_process | proton transmembrane transport |
B | 0004129 | molecular_function | cytochrome-c oxidase activity |
B | 0005507 | molecular_function | copper ion binding |
B | 0005509 | molecular_function | calcium ion binding |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019333 | biological_process | denitrification pathway |
B | 0042597 | cellular_component | periplasmic space |
B | 0046872 | molecular_function | metal ion binding |
B | 0050304 | molecular_function | nitrous-oxide reductase activity |
B | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA A 1001 |
Chain | Residue |
A | TYR252 |
A | GLU255 |
A | MET263 |
A | ASP269 |
A | SER316 |
A | HOH1209 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue BU3 A 1002 |
Chain | Residue |
A | GLU267 |
A | ARG268 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue BU3 A 1003 |
Chain | Residue |
A | MET131 |
A | ASN137 |
A | LYS139 |
A | TYR183 |
A | THR184 |
A | GLU221 |
A | HOH1415 |
A | SER130 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue BU3 A 1004 |
Chain | Residue |
A | ILE105 |
A | HIS581 |
A | THR596 |
A | PHE597 |
A | HOH1127 |
A | HOH1128 |
B | MET120 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue BU3 A 1005 |
Chain | Residue |
A | GLN429 |
A | LYS494 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 1006 |
Chain | Residue |
A | HIS491 |
A | ARG492 |
A | HOH1194 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue CA B 1001 |
Chain | Residue |
B | TYR252 |
B | GLU255 |
B | MET263 |
B | ASP269 |
B | SER316 |
B | HOH1145 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue BU3 B 1002 |
Chain | Residue |
B | SER130 |
B | MET131 |
B | ASN137 |
B | TYR183 |
B | THR184 |
B | GLU221 |
B | HOH1375 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 1003 |
Chain | Residue |
B | HIS491 |
B | ARG492 |
B | HOH1125 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue SO4 B 1004 |
Chain | Residue |
B | GLY104 |
B | ALA117 |
Functional Information from PROSITE/UniProt
site_id | PS00078 |
Number of Residues | 49 |
Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VtHgfcmtnhgvqmevapqatasvtfiankpgvqwyy......CnwfChalHmeM |
Chain | Residue | Details |
A | VAL572-MET620 | |