3OMA
Catalytic core subunits (I and II) of cytochrome C oxidase from Rhodobacter sphaeroides with K362M mutation
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 | 0015990 | biological_process | electron transport coupled proton transport |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
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 |
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 | 0016491 | molecular_function | oxidoreductase activity |
B | 0022900 | biological_process | electron transport chain |
B | 0042773 | biological_process | ATP synthesis coupled electron transport |
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 | 0006119 | biological_process | oxidative phosphorylation |
C | 0009060 | biological_process | aerobic respiration |
C | 0015990 | biological_process | electron transport coupled proton transport |
C | 0016020 | cellular_component | membrane |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0020037 | molecular_function | heme binding |
C | 0022904 | biological_process | respiratory electron transport chain |
C | 0045277 | cellular_component | respiratory chain complex IV |
C | 0046872 | molecular_function | metal ion binding |
D | 0004129 | molecular_function | cytochrome-c oxidase activity |
D | 0005507 | molecular_function | copper ion binding |
D | 0005886 | cellular_component | plasma membrane |
D | 0016020 | cellular_component | membrane |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0022900 | biological_process | electron transport chain |
D | 0042773 | biological_process | ATP synthesis coupled electron transport |
D | 0046872 | molecular_function | metal ion binding |
D | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE OH A 706 |
Chain | Residue |
A | HEA2 |
A | CU5 |
A | HIS284 |
A | VAL287 |
A | HIS334 |
A | HOH727 |
A | HOH806 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMU A 1005 |
Chain | Residue |
A | GLN61 |
A | PHE502 |
A | TRD552 |
A | HOH771 |
A | MET56 |
A | ALA57 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMU A 7 |
Chain | Residue |
A | LEU34 |
A | MET443 |
A | SER444 |
A | HOH769 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE TRD A 1013 |
Chain | Residue |
A | PHE76 |
A | SER79 |
site_id | AC5 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE HEA A 1 |
Chain | Residue |
A | LEU34 |
A | VAL45 |
A | THR48 |
A | MET51 |
A | ARG52 |
A | TRP95 |
A | ILE99 |
A | HIS102 |
A | MET106 |
A | MET107 |
A | VAL111 |
A | GLY171 |
A | TRP172 |
A | TYR414 |
A | HIS421 |
A | SER425 |
A | MET460 |
A | PHE468 |
A | GLN471 |
A | ARG481 |
A | ARG482 |
A | SER504 |
A | PHE508 |
A | HOH720 |
A | HOH722 |
A | HOH780 |
site_id | AC6 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE HEA A 2 |
Chain | Residue |
A | HOH15 |
A | TRP172 |
A | TRP280 |
A | VAL287 |
A | TYR288 |
A | HIS333 |
A | HIS334 |
A | THR352 |
A | ILE355 |
A | THR359 |
A | GLY360 |
A | GLY395 |
A | GLY398 |
A | ILE399 |
A | LEU401 |
A | SER402 |
A | ASP407 |
A | HIS411 |
A | VAL416 |
A | HIS419 |
A | PHE420 |
A | VAL423 |
A | MET424 |
A | ARG481 |
A | OH706 |
A | HOH727 |
A | HOH735 |
A | HOH765 |
B | ILE68 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE TRD A 552 |
Chain | Residue |
A | LEU80 |
A | TRP81 |
A | PRO82 |
A | DMU1005 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE TRD A 3 |
Chain | Residue |
A | ARG476 |
B | THR41 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU A 5 |
Chain | Residue |
A | HIS284 |
A | HIS333 |
A | HIS334 |
A | OH706 |
A | HOH727 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 6 |
Chain | Residue |
A | HIS411 |
A | ASP412 |
B | GLU254 |
B | HOH738 |
B | HOH744 |
B | HOH750 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 553 |
Chain | Residue |
A | GLU54 |
A | ALA57 |
A | GLY59 |
A | GLN61 |
A | HOH758 |
A | HOH771 |
site_id | BC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE DMU B 1 |
Chain | Residue |
A | GLY513 |
A | TYR517 |
B | DMU2 |
B | HOH26 |
B | GLN142 |
B | TRP143 |
B | PRO164 |
B | HOH730 |
B | HOH737 |
A | TRP451 |
A | PHE510 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMU B 2 |
Chain | Residue |
A | TRP451 |
A | HOH835 |
B | DMU1 |
site_id | BC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DMU B 3 |
Chain | Residue |
A | TRP371 |
B | LEU75 |
B | HIS96 |
B | ASN97 |
D | SER173 |
D | PRO174 |
D | GLU177 |
D | HOH356 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMU B 6 |
Chain | Residue |
B | PHE124 |
B | ASN125 |
B | GLU128 |
site_id | BC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE HTH B 286 |
Chain | Residue |
B | GLU152 |
B | GLU153 |
B | ALA276 |
B | GLU280 |
B | HIS283 |
B | HOH496 |
B | HOH715 |
D | ALA276 |
D | GLU280 |
D | HIS283 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU B 287 |
Chain | Residue |
B | CYS252 |
B | GLU254 |
B | CYS256 |
B | HIS260 |
B | CU1288 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU1 B 288 |
Chain | Residue |
B | HIS217 |
B | CYS252 |
B | CYS256 |
B | MET263 |
B | CU287 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD B 8 |
Chain | Residue |
B | GLU280 |
B | HIS283 |
B | HIS285 |
D | GLU152 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD B 9 |
Chain | Residue |
B | HIS96 |
B | GLU101 |
B | HOH714 |
B | HOH801 |
B | HOH802 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE OH C 706 |
Chain | Residue |
C | HEA2 |
C | HIS284 |
C | VAL287 |
C | HIS334 |
C | CU553 |
C | HOH556 |
site_id | CC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DMU C 10 |
Chain | Residue |
C | ALA57 |
C | GLN61 |
C | SER83 |
C | VAL85 |
C | PHE502 |
C | TRD552 |
C | HOH597 |
site_id | CC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE DMU C 5 |
Chain | Residue |
C | TRP451 |
site_id | CC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE DMU C 9 |
Chain | Residue |
C | MET443 |
site_id | CC7 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE HEA C 1 |
Chain | Residue |
C | HOH3 |
C | LEU34 |
C | GLY38 |
C | THR48 |
C | MET51 |
C | ARG52 |
C | TRP95 |
C | ILE99 |
C | HIS102 |
C | MET106 |
C | MET107 |
C | VAL111 |
C | GLY171 |
C | TRP172 |
C | TYR414 |
C | HIS421 |
C | MET424 |
C | SER425 |
C | VAL429 |
C | MET460 |
C | PHE468 |
C | GLN471 |
C | ARG481 |
C | ARG482 |
C | SER504 |
C | PHE508 |
C | HOH554 |
C | HOH606 |
site_id | CC8 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE HEA C 2 |
Chain | Residue |
C | HOH15 |
C | TRP172 |
C | TRP280 |
C | VAL287 |
C | TYR288 |
C | HIS333 |
C | HIS334 |
C | THR352 |
C | ILE355 |
C | THR359 |
C | GLY360 |
C | GLY395 |
C | GLY398 |
C | LEU401 |
C | SER402 |
C | ASP407 |
C | HIS411 |
C | VAL416 |
C | HIS419 |
C | PHE420 |
C | VAL423 |
C | MET424 |
C | ARG481 |
C | HOH556 |
C | HOH565 |
C | HOH593 |
C | OH706 |
site_id | CC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE TRD C 552 |
Chain | Residue |
C | DMU10 |
C | LEU80 |
C | TRP81 |
C | PRO82 |
site_id | DC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU C 553 |
Chain | Residue |
C | HIS284 |
C | HIS333 |
C | HIS334 |
C | HOH556 |
C | OH706 |
site_id | DC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 6 |
Chain | Residue |
C | HIS411 |
C | ASP412 |
C | HOH585 |
D | GLU254 |
D | HOH316 |
D | HOH327 |
site_id | DC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 7 |
Chain | Residue |
C | GLU54 |
C | ALA57 |
C | GLY59 |
C | GLN61 |
C | HOH586 |
C | HOH597 |
site_id | DC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMU D 4 |
Chain | Residue |
D | PRO121 |
D | PHE124 |
D | GLU128 |
site_id | DC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE DMU D 8 |
Chain | Residue |
D | HIS96 |
D | ASN97 |
site_id | DC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE TRD D 3 |
Chain | Residue |
C | HIS472 |
C | ARG476 |
D | THR41 |
site_id | DC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE TRD D 14 |
Chain | Residue |
C | MET353 |
D | LEU112 |
site_id | DC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU D 286 |
Chain | Residue |
D | CYS252 |
D | GLU254 |
D | CYS256 |
D | HIS260 |
D | CU1287 |
site_id | DC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU1 D 287 |
Chain | Residue |
D | HIS217 |
D | CYS252 |
D | CYS256 |
D | MET263 |
D | CU286 |
site_id | EC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD D 288 |
Chain | Residue |
B | GLU152 |
D | GLU280 |
D | HIS283 |
D | HIS285 |
site_id | EC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD D 9 |
Chain | Residue |
D | HIS96 |
D | GLU101 |
D | HOH375 |
D | HOH376 |
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. WFFGHPeVyiivlpafgivshviatfakkpifgylpmvyamvaigvlgfvvwa..HH |
Chain | Residue | Details |
A | TRP280-HIS334 |
site_id | PS00078 |
Number of Residues | 49 |
Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHswtvpafgvkqdavpgrlaqlwfraeregiffgq......CselCgisHayM |
Chain | Residue | Details |
B | VAL215-MET263 |