3MK7
The structure of CBB3 cytochrome oxidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004129 | molecular_function | cytochrome-c oxidase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006119 | biological_process | oxidative phosphorylation |
| A | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| A | 0009060 | biological_process | aerobic respiration |
| A | 0015078 | molecular_function | proton transmembrane transporter activity |
| A | 0015990 | biological_process | electron transport coupled proton transport |
| A | 0016020 | cellular_component | membrane |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0019411 | biological_process | aerobic respiration, using ferrous ions as electron donor |
| A | 0019646 | biological_process | aerobic electron transport chain |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070069 | cellular_component | cytochrome complex |
| A | 0098803 | cellular_component | respiratory chain complex |
| A | 1902600 | biological_process | proton transmembrane transport |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070069 | cellular_component | cytochrome complex |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006119 | biological_process | oxidative phosphorylation |
| C | 0006811 | biological_process | monoatomic ion transport |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070069 | cellular_component | cytochrome complex |
| C | 1902600 | biological_process | proton transmembrane transport |
| D | 0004129 | molecular_function | cytochrome-c oxidase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005507 | molecular_function | copper ion binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006119 | biological_process | oxidative phosphorylation |
| D | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| D | 0009060 | biological_process | aerobic respiration |
| D | 0015078 | molecular_function | proton transmembrane transporter activity |
| D | 0015990 | biological_process | electron transport coupled proton transport |
| D | 0016020 | cellular_component | membrane |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0019411 | biological_process | aerobic respiration, using ferrous ions as electron donor |
| D | 0019646 | biological_process | aerobic electron transport chain |
| D | 0019825 | molecular_function | oxygen binding |
| D | 0020037 | molecular_function | heme binding |
| D | 0022904 | biological_process | respiratory electron transport chain |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0070069 | cellular_component | cytochrome complex |
| D | 0098803 | cellular_component | respiratory chain complex |
| D | 1902600 | biological_process | proton transmembrane transport |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0070069 | cellular_component | cytochrome complex |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0006119 | biological_process | oxidative phosphorylation |
| F | 0006811 | biological_process | monoatomic ion transport |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0020037 | molecular_function | heme binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0070069 | cellular_component | cytochrome complex |
| F | 1902600 | biological_process | proton transmembrane transport |
| G | 0004129 | molecular_function | cytochrome-c oxidase activity |
| G | 0005506 | molecular_function | iron ion binding |
| G | 0005507 | molecular_function | copper ion binding |
| G | 0005886 | cellular_component | plasma membrane |
| G | 0006119 | biological_process | oxidative phosphorylation |
| G | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| G | 0009060 | biological_process | aerobic respiration |
| G | 0015078 | molecular_function | proton transmembrane transporter activity |
| G | 0015990 | biological_process | electron transport coupled proton transport |
| G | 0016020 | cellular_component | membrane |
| G | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| G | 0019411 | biological_process | aerobic respiration, using ferrous ions as electron donor |
| G | 0019646 | biological_process | aerobic electron transport chain |
| G | 0019825 | molecular_function | oxygen binding |
| G | 0020037 | molecular_function | heme binding |
| G | 0022904 | biological_process | respiratory electron transport chain |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0070069 | cellular_component | cytochrome complex |
| G | 0098803 | cellular_component | respiratory chain complex |
| G | 1902600 | biological_process | proton transmembrane transport |
| H | 0009055 | molecular_function | electron transfer activity |
| H | 0020037 | molecular_function | heme binding |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0070069 | cellular_component | cytochrome complex |
| I | 0005886 | cellular_component | plasma membrane |
| I | 0006119 | biological_process | oxidative phosphorylation |
| I | 0006811 | biological_process | monoatomic ion transport |
| I | 0009055 | molecular_function | electron transfer activity |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0020037 | molecular_function | heme binding |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0070069 | cellular_component | cytochrome complex |
| I | 1902600 | biological_process | proton transmembrane transport |
| K | 0004129 | molecular_function | cytochrome-c oxidase activity |
| K | 0005506 | molecular_function | iron ion binding |
| K | 0005507 | molecular_function | copper ion binding |
| K | 0005886 | cellular_component | plasma membrane |
| K | 0006119 | biological_process | oxidative phosphorylation |
| K | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| K | 0009060 | biological_process | aerobic respiration |
| K | 0015078 | molecular_function | proton transmembrane transporter activity |
| K | 0015990 | biological_process | electron transport coupled proton transport |
| K | 0016020 | cellular_component | membrane |
| K | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| K | 0019411 | biological_process | aerobic respiration, using ferrous ions as electron donor |
| K | 0019646 | biological_process | aerobic electron transport chain |
| K | 0019825 | molecular_function | oxygen binding |
| K | 0020037 | molecular_function | heme binding |
| K | 0022904 | biological_process | respiratory electron transport chain |
| K | 0046872 | molecular_function | metal ion binding |
| K | 0070069 | cellular_component | cytochrome complex |
| K | 0098803 | cellular_component | respiratory chain complex |
| K | 1902600 | biological_process | proton transmembrane transport |
| L | 0009055 | molecular_function | electron transfer activity |
| L | 0020037 | molecular_function | heme binding |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0070069 | cellular_component | cytochrome complex |
| M | 0005886 | cellular_component | plasma membrane |
| M | 0006119 | biological_process | oxidative phosphorylation |
| M | 0006811 | biological_process | monoatomic ion transport |
| M | 0009055 | molecular_function | electron transfer activity |
| M | 0016491 | molecular_function | oxidoreductase activity |
| M | 0020037 | molecular_function | heme binding |
| M | 0046872 | molecular_function | metal ion binding |
| M | 0070069 | cellular_component | cytochrome complex |
| M | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | GLU122 |
| A | THR321 |
| A | GLY324 |
| A | PRO325 |
| A | MET327 |
| A | ALA328 |
| A | ASN333 |
| A | HIS337 |
| A | HIS345 |
| A | VAL346 |
| A | GLY349 |
| A | TYR123 |
| A | HEM502 |
| A | PEO508 |
| B | SER102 |
| B | CA504 |
| A | TRP203 |
| A | VAL210 |
| A | LEU214 |
| A | TYR251 |
| A | HIS257 |
| A | SER283 |
| A | SER320 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 502 |
| Chain | Residue |
| A | MET29 |
| A | GLY32 |
| A | VAL33 |
| A | ALA36 |
| A | ARG57 |
| A | HIS60 |
| A | THR61 |
| A | VAL64 |
| A | GLU122 |
| A | TYR123 |
| A | ASP340 |
| A | ILE343 |
| A | VAL346 |
| A | HIS347 |
| A | ALA350 |
| A | LEU351 |
| A | TYR395 |
| A | ARG437 |
| A | GLY441 |
| A | HEM501 |
| B | LYS103 |
| B | CA504 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 503 |
| Chain | Residue |
| A | HIS207 |
| A | HIS257 |
| A | HIS258 |
| A | PEO508 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 504 |
| Chain | Residue |
| A | ARG57 |
| A | GLU122 |
| A | HEM501 |
| A | HEM502 |
| B | SER102 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 505 |
| Chain | Residue |
| A | ALA124 |
| A | LEU126 |
| A | ASP131 |
| A | ASN179 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEO A 508 |
| Chain | Residue |
| A | HIS207 |
| A | VAL210 |
| A | HIS258 |
| A | HEM501 |
| A | CU503 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 506 |
| Chain | Residue |
| A | MET273 |
| A | ILE329 |
| A | LYS330 |
| A | THR331 |
| C | TYR72 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC B 211 |
| Chain | Residue |
| A | PHE53 |
| A | LEU427 |
| B | CYS65 |
| B | CYS68 |
| B | HIS69 |
| B | THR105 |
| B | GLY106 |
| B | PRO107 |
| B | LEU109 |
| B | VAL112 |
| B | TYR116 |
| B | HIS121 |
| B | HIS124 |
| B | LEU125 |
| B | VAL132 |
| B | SER135 |
| B | LYS136 |
| B | MET137 |
| B | PRO138 |
| B | TYR140 |
| B | MET188 |
| site_id | AC9 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEC C 321 |
| Chain | Residue |
| C | LEU247 |
| C | GLY248 |
| C | ALA249 |
| C | PRO250 |
| C | TRP258 |
| C | ILE259 |
| C | TYR260 |
| C | LEU267 |
| C | THR270 |
| C | ILE271 |
| C | ARG275 |
| C | GLY277 |
| C | HEC322 |
| I | ILE183 |
| C | ARG166 |
| C | ALA184 |
| C | ALA185 |
| C | MET186 |
| C | PRO187 |
| C | TRP189 |
| C | THR232 |
| C | CYS233 |
| C | CYS236 |
| C | HIS237 |
| site_id | BC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC C 322 |
| Chain | Residue |
| B | TYR116 |
| B | SER117 |
| C | TYR142 |
| C | CYS143 |
| C | CYS146 |
| C | HIS147 |
| C | GLY156 |
| C | PHE157 |
| C | PRO158 |
| C | TRP165 |
| C | ARG166 |
| C | TRP167 |
| C | ILE178 |
| C | ALA184 |
| C | GLY277 |
| C | GLN278 |
| C | MET279 |
| C | PRO280 |
| C | HEC321 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FC6 M 323 |
| Chain | Residue |
| C | ARG206 |
| C | PRO215 |
| C | SER263 |
| C | LEU264 |
| M | GLY265 |
| M | GLN266 |
| M | GLN269 |
| M | ARG275 |
| site_id | BC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM D 501 |
| Chain | Residue |
| D | GLU122 |
| D | TYR123 |
| D | TRP203 |
| D | VAL210 |
| D | LEU214 |
| D | TYR251 |
| D | HIS257 |
| D | SER283 |
| D | SER320 |
| D | THR321 |
| D | GLY324 |
| D | PRO325 |
| D | MET327 |
| D | ALA328 |
| D | ASN333 |
| D | HIS337 |
| D | HIS345 |
| D | VAL346 |
| D | GLY349 |
| D | HEM502 |
| D | PEO508 |
| E | SER102 |
| E | CA504 |
| site_id | BC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM D 502 |
| Chain | Residue |
| D | MET29 |
| D | GLY32 |
| D | VAL33 |
| D | ALA36 |
| D | ARG57 |
| D | HIS60 |
| D | THR61 |
| D | VAL64 |
| D | GLU122 |
| D | TYR123 |
| D | ASP340 |
| D | THR342 |
| D | ILE343 |
| D | VAL346 |
| D | HIS347 |
| D | ALA350 |
| D | LEU351 |
| D | TYR395 |
| D | ARG437 |
| D | GLY441 |
| D | HEM501 |
| E | LYS103 |
| E | CA504 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU D 503 |
| Chain | Residue |
| D | HIS207 |
| D | HIS257 |
| D | HIS258 |
| D | PEO508 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA E 504 |
| Chain | Residue |
| D | ARG57 |
| D | GLU122 |
| D | HEM501 |
| D | HEM502 |
| E | SER102 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 505 |
| Chain | Residue |
| D | ALA124 |
| D | LEU126 |
| D | ASP131 |
| D | ASN179 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 D 506 |
| Chain | Residue |
| D | MET273 |
| D | ILE329 |
| D | LYS330 |
| D | THR331 |
| F | TYR72 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEO D 508 |
| Chain | Residue |
| D | HIS207 |
| D | VAL210 |
| D | HIS258 |
| D | HEM501 |
| D | CU503 |
| site_id | CC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEC E 211 |
| Chain | Residue |
| D | LEU427 |
| E | CYS65 |
| E | CYS68 |
| E | HIS69 |
| E | THR105 |
| E | GLY106 |
| E | PRO107 |
| E | LEU109 |
| E | TYR116 |
| E | HIS121 |
| E | HIS124 |
| E | LEU125 |
| E | VAL132 |
| E | SER135 |
| E | LYS136 |
| E | MET137 |
| E | PRO138 |
| E | TYR140 |
| site_id | CC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC F 321 |
| Chain | Residue |
| F | ARG166 |
| F | ALA184 |
| F | ALA185 |
| F | MET186 |
| F | TRP189 |
| F | THR232 |
| F | CYS233 |
| F | CYS236 |
| F | HIS237 |
| F | LEU247 |
| F | GLY248 |
| F | ALA249 |
| F | PRO250 |
| F | TRP258 |
| F | ILE259 |
| F | TYR260 |
| F | LEU267 |
| F | THR270 |
| F | ILE271 |
| F | ARG275 |
| F | GLY277 |
| F | HEC322 |
| site_id | CC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC F 322 |
| Chain | Residue |
| E | TYR116 |
| E | SER117 |
| F | TYR142 |
| F | CYS143 |
| F | CYS146 |
| F | HIS147 |
| F | GLY156 |
| F | PRO158 |
| F | LEU160 |
| F | TRP165 |
| F | ARG166 |
| F | TRP167 |
| F | ILE178 |
| F | ALA184 |
| F | GLY277 |
| F | GLN278 |
| F | MET279 |
| F | PRO280 |
| F | GLN282 |
| F | LEU286 |
| F | HEC321 |
| site_id | CC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FC6 I 323 |
| Chain | Residue |
| F | ARG206 |
| F | PRO215 |
| F | SER263 |
| F | LEU264 |
| I | GLY265 |
| I | GLN266 |
| I | GLN269 |
| I | ARG275 |
| site_id | CC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM G 501 |
| Chain | Residue |
| G | GLU122 |
| G | TYR123 |
| G | TRP203 |
| G | VAL210 |
| G | LEU214 |
| G | TYR251 |
| G | HIS257 |
| G | SER283 |
| G | SER320 |
| G | GLY324 |
| G | PRO325 |
| G | MET327 |
| G | ALA328 |
| G | ASN333 |
| G | HIS337 |
| G | HIS345 |
| G | VAL346 |
| G | GLY349 |
| G | HEM502 |
| G | CA504 |
| G | PEO508 |
| H | SER102 |
| site_id | CC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM G 502 |
| Chain | Residue |
| G | MET29 |
| G | GLY32 |
| G | VAL33 |
| G | ILE35 |
| G | ALA36 |
| G | ARG57 |
| G | HIS60 |
| G | THR61 |
| G | VAL64 |
| G | GLU122 |
| G | TYR123 |
| G | ASP340 |
| G | THR342 |
| G | ILE343 |
| G | VAL346 |
| G | HIS347 |
| G | ALA350 |
| G | LEU351 |
| G | TYR395 |
| G | ARG437 |
| G | HEM501 |
| G | CA504 |
| H | LYS103 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU G 503 |
| Chain | Residue |
| G | HIS207 |
| G | HIS257 |
| G | HIS258 |
| G | PEO508 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA G 504 |
| Chain | Residue |
| G | ARG57 |
| G | GLU122 |
| G | HEM501 |
| G | HEM502 |
| H | SER102 |
| site_id | CC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA G 505 |
| Chain | Residue |
| G | ALA124 |
| G | LEU126 |
| G | ASP131 |
| G | ASN179 |
| site_id | DC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEO G 508 |
| Chain | Residue |
| G | HIS207 |
| G | VAL210 |
| G | HIS258 |
| G | HEM501 |
| G | CU503 |
| site_id | DC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 G 506 |
| Chain | Residue |
| G | MET273 |
| G | ILE329 |
| G | LYS330 |
| G | THR331 |
| I | TYR72 |
| site_id | DC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEC H 211 |
| Chain | Residue |
| H | CYS65 |
| H | CYS68 |
| H | HIS69 |
| H | THR105 |
| H | GLY106 |
| H | PRO107 |
| H | LEU109 |
| H | VAL112 |
| H | TYR116 |
| H | HIS121 |
| H | HIS124 |
| H | LEU125 |
| H | VAL132 |
| H | SER135 |
| H | LYS136 |
| H | MET137 |
| H | PRO138 |
| H | TYR140 |
| site_id | DC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEC I 321 |
| Chain | Residue |
| C | ILE183 |
| I | ARG166 |
| I | ALA184 |
| I | ALA185 |
| I | MET186 |
| I | PRO187 |
| I | TRP189 |
| I | THR232 |
| I | CYS233 |
| I | CYS236 |
| I | HIS237 |
| I | LEU247 |
| I | GLY248 |
| I | ALA249 |
| I | PRO250 |
| I | TRP258 |
| I | ILE259 |
| I | TYR260 |
| I | LEU267 |
| I | THR270 |
| I | ILE271 |
| I | GLY277 |
| I | HEC322 |
| site_id | DC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEC I 322 |
| Chain | Residue |
| H | TYR116 |
| H | SER117 |
| I | TYR142 |
| I | CYS143 |
| I | CYS146 |
| I | HIS147 |
| I | GLY156 |
| I | PHE157 |
| I | PRO158 |
| I | LEU160 |
| I | TRP165 |
| I | ARG166 |
| I | TRP167 |
| I | ILE178 |
| I | ALA184 |
| I | GLY277 |
| I | GLN278 |
| I | MET279 |
| I | PRO280 |
| I | HEC321 |
| site_id | DC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FC6 F 323 |
| Chain | Residue |
| F | GLY265 |
| F | GLN266 |
| F | GLN269 |
| F | ARG275 |
| I | ARG206 |
| I | PRO215 |
| I | SER263 |
| I | LEU264 |
| site_id | DC7 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM K 501 |
| Chain | Residue |
| K | GLU122 |
| K | TYR123 |
| K | TRP203 |
| K | VAL210 |
| K | LEU214 |
| K | TYR251 |
| K | HIS257 |
| K | SER283 |
| K | SER320 |
| K | THR321 |
| K | GLY324 |
| K | PRO325 |
| K | MET327 |
| K | ALA328 |
| K | ASN333 |
| K | HIS337 |
| K | THR342 |
| K | HIS345 |
| K | VAL346 |
| K | GLY349 |
| K | HEM502 |
| K | CA504 |
| K | PEO508 |
| L | SER102 |
| site_id | DC8 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEM K 502 |
| Chain | Residue |
| K | MET29 |
| K | GLY32 |
| K | VAL33 |
| K | ILE35 |
| K | ALA36 |
| K | ARG57 |
| K | HIS60 |
| K | THR61 |
| K | VAL64 |
| K | ILE65 |
| K | GLU122 |
| K | TYR123 |
| K | ASP340 |
| K | THR342 |
| K | ILE343 |
| K | VAL346 |
| K | HIS347 |
| K | ALA350 |
| K | LEU351 |
| K | TYR395 |
| K | ARG437 |
| K | GLY441 |
| K | PHE444 |
| K | HEM501 |
| K | CA504 |
| L | LYS103 |
| site_id | DC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU K 503 |
| Chain | Residue |
| K | HIS207 |
| K | HIS257 |
| K | HIS258 |
| K | PEO508 |
| site_id | EC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA K 504 |
| Chain | Residue |
| K | ARG57 |
| K | GLU122 |
| K | HEM501 |
| K | HEM502 |
| L | SER102 |
| site_id | EC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA K 505 |
| Chain | Residue |
| K | ALA124 |
| K | LEU126 |
| K | ASP131 |
| K | ASN179 |
| site_id | EC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 K 506 |
| Chain | Residue |
| K | MET273 |
| K | ILE329 |
| K | LYS330 |
| K | THR331 |
| M | TYR72 |
| site_id | EC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEO K 508 |
| Chain | Residue |
| K | HIS207 |
| K | VAL210 |
| K | HIS258 |
| K | HEM501 |
| K | CU503 |
| site_id | EC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEC L 211 |
| Chain | Residue |
| L | GLU63 |
| L | CYS65 |
| L | CYS68 |
| L | HIS69 |
| L | THR105 |
| L | GLY106 |
| L | PRO107 |
| L | LEU109 |
| L | VAL112 |
| L | TYR116 |
| L | HIS121 |
| L | HIS124 |
| L | LEU125 |
| L | VAL132 |
| L | SER135 |
| L | LYS136 |
| L | MET137 |
| L | PRO138 |
| L | TYR140 |
| L | MET188 |
| site_id | EC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEC M 321 |
| Chain | Residue |
| M | ARG166 |
| M | ILE183 |
| M | ALA184 |
| M | ALA185 |
| M | MET186 |
| M | TRP189 |
| M | THR232 |
| M | CYS233 |
| M | CYS236 |
| M | HIS237 |
| M | LEU247 |
| M | GLY248 |
| M | ALA249 |
| M | PRO250 |
| M | TRP258 |
| M | ILE259 |
| M | TYR260 |
| M | LEU267 |
| M | THR270 |
| M | ILE271 |
| M | ARG275 |
| M | GLY277 |
| M | HEC322 |
| site_id | EC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC M 322 |
| Chain | Residue |
| L | TYR116 |
| L | SER117 |
| M | TYR142 |
| M | CYS143 |
| M | CYS146 |
| M | HIS147 |
| M | GLY156 |
| M | PHE157 |
| M | PRO158 |
| M | LEU160 |
| M | TRP165 |
| M | ARG166 |
| M | TRP167 |
| M | ILE178 |
| M | ALA184 |
| M | GLY277 |
| M | GLN278 |
| M | MET279 |
| M | PRO280 |
| M | GLN282 |
| M | HEC321 |
| site_id | EC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FC6 C 323 |
| Chain | Residue |
| C | GLY265 |
| C | GLN266 |
| C | GLN269 |
| C | ARG275 |
| M | ARG206 |
| M | PRO215 |
| M | SER263 |
| M | LEU264 |
Functional Information from PROSITE/UniProt
| site_id | PS00077 |
| Number of Residues | 56 |
| Details | COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WWYGHNaVgffltagflgimyyfvpkqaerpvysyrlsivhfwalitvyiwagp.HH |
| Chain | Residue | Details |
| A | TRP203-HIS258 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 960 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 444 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 252 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20576851","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MK7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20576851","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MK7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 160 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"20576851","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 316 |
| Details | Domain: {"description":"Cytochrome c 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 328 |
| Details | Domain: {"description":"Cytochrome c 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"20576851","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20576851","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
