1M57
Structure of cytochrome c oxidase from Rhodobacter sphaeroides (EQ(I-286) mutant))
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004129 | molecular_function | cytochrome-c oxidase activity |
| A | 0005515 | molecular_function | protein binding |
| 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 | 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 |
| A | 0070469 | cellular_component | respirasome |
| A | 1902600 | biological_process | proton transmembrane transport |
| B | 0004129 | molecular_function | cytochrome-c oxidase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005515 | molecular_function | protein 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 | 0046872 | molecular_function | metal ion binding |
| B | 0070469 | cellular_component | respirasome |
| B | 1902600 | biological_process | proton transmembrane transport |
| C | 0004129 | molecular_function | cytochrome-c oxidase activity |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0009060 | biological_process | aerobic respiration |
| C | 0016020 | cellular_component | membrane |
| C | 0019646 | biological_process | aerobic electron transport chain |
| C | 0022904 | biological_process | respiratory electron transport chain |
| C | 1902600 | biological_process | proton transmembrane transport |
| G | 0004129 | molecular_function | cytochrome-c oxidase activity |
| G | 0005515 | molecular_function | protein binding |
| G | 0005886 | cellular_component | plasma membrane |
| G | 0006119 | biological_process | oxidative phosphorylation |
| G | 0009060 | biological_process | aerobic respiration |
| G | 0015990 | biological_process | electron transport coupled proton transport |
| G | 0016020 | cellular_component | membrane |
| G | 0020037 | molecular_function | heme binding |
| G | 0022904 | biological_process | respiratory electron transport chain |
| G | 0045277 | cellular_component | respiratory chain complex IV |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0070469 | cellular_component | respirasome |
| G | 1902600 | biological_process | proton transmembrane transport |
| H | 0004129 | molecular_function | cytochrome-c oxidase activity |
| H | 0005507 | molecular_function | copper ion binding |
| H | 0005515 | molecular_function | protein binding |
| H | 0005886 | cellular_component | plasma membrane |
| H | 0016020 | cellular_component | membrane |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0022900 | biological_process | electron transport chain |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0070469 | cellular_component | respirasome |
| H | 1902600 | biological_process | proton transmembrane transport |
| I | 0004129 | molecular_function | cytochrome-c oxidase activity |
| I | 0005886 | cellular_component | plasma membrane |
| I | 0009055 | molecular_function | electron transfer activity |
| I | 0009060 | biological_process | aerobic respiration |
| I | 0016020 | cellular_component | membrane |
| I | 0019646 | biological_process | aerobic electron transport chain |
| I | 0022904 | biological_process | respiratory electron transport chain |
| I | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU B 1003 |
| Chain | Residue |
| B | CYS252 |
| B | GLU254 |
| B | CYS256 |
| B | HIS260 |
| B | CU1004 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU B 1004 |
| Chain | Residue |
| B | CU1003 |
| B | HIS217 |
| B | CYS252 |
| B | CYS256 |
| B | MET263 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CU A 1005 |
| Chain | Residue |
| A | HIS284 |
| A | HIS333 |
| A | HIS334 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG A 2006 |
| Chain | Residue |
| A | HIS411 |
| A | ASP412 |
| A | HOH2057 |
| A | HOH2103 |
| B | GLU254 |
| B | HOH1009 |
| B | HOH1010 |
| B | HOH1012 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1007 |
| Chain | Residue |
| A | GLU54 |
| A | ALA57 |
| A | PRO58 |
| A | GLY59 |
| A | GLN61 |
| A | HOH2058 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU H 1003 |
| Chain | Residue |
| H | CYS252 |
| H | GLU254 |
| H | CYS256 |
| H | HIS260 |
| H | CU1004 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU H 1004 |
| Chain | Residue |
| H | HIS217 |
| H | CYS252 |
| H | CYS256 |
| H | MET263 |
| H | CU1003 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CU G 1005 |
| Chain | Residue |
| G | HIS284 |
| G | HIS333 |
| G | HIS334 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG G 3006 |
| Chain | Residue |
| G | HIS411 |
| G | ASP412 |
| G | HOH3062 |
| G | HOH3115 |
| H | GLU254 |
| H | HOH1050 |
| H | HOH1051 |
| H | HOH1054 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA G 1007 |
| Chain | Residue |
| G | GLU54 |
| G | ALA57 |
| G | PRO58 |
| G | GLY59 |
| G | GLN61 |
| G | HOH3063 |
| site_id | BC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEA A 1001 |
| Chain | Residue |
| A | GLY37 |
| A | GLY38 |
| A | THR48 |
| A | MET51 |
| A | ARG52 |
| A | TRP95 |
| A | ILE99 |
| A | HIS102 |
| A | GLY103 |
| A | MET106 |
| A | TRP172 |
| A | TYR414 |
| A | PHE420 |
| A | HIS421 |
| A | MET424 |
| A | VAL429 |
| A | ILE432 |
| A | THR467 |
| A | PHE468 |
| A | GLN471 |
| A | ARG481 |
| A | ARG482 |
| A | SER504 |
| A | PHE508 |
| A | HOH2019 |
| A | HOH2054 |
| site_id | BC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEA A 1002 |
| Chain | Residue |
| A | ARG481 |
| A | HOH2015 |
| A | HOH2022 |
| A | HOH2047 |
| B | ILE68 |
| A | MET107 |
| A | TRP172 |
| A | TRP280 |
| A | VAL287 |
| A | TYR288 |
| A | HIS333 |
| A | HIS334 |
| A | THR359 |
| A | GLY360 |
| A | GLY398 |
| A | LEU401 |
| A | SER402 |
| A | ASP407 |
| A | HIS411 |
| A | VAL416 |
| A | HIS419 |
| A | PHE420 |
| A | VAL423 |
| A | MET424 |
| site_id | BC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE 3PE C 2008 |
| Chain | Residue |
| A | 3PE2009 |
| C | LEU52 |
| C | MET55 |
| C | TRP59 |
| C | VAL62 |
| C | VAL63 |
| C | SER66 |
| C | LEU67 |
| C | HIS71 |
| C | PHE83 |
| C | PHE86 |
| C | PHE219 |
| C | VAL222 |
| C | ARG226 |
| C | HIS231 |
| C | PHE232 |
| C | VAL238 |
| C | GLY239 |
| C | HOH2040 |
| site_id | BC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 3PE A 2009 |
| Chain | Residue |
| A | PHE135 |
| A | PRO136 |
| A | ARG137 |
| A | MET138 |
| A | LEU145 |
| A | ALA247 |
| C | MET55 |
| C | TRP58 |
| C | TRP59 |
| C | GLY82 |
| C | PHE83 |
| C | PHE86 |
| C | 3PE2008 |
| site_id | BC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 3PE C 2010 |
| Chain | Residue |
| A | PHE281 |
| A | TRP331 |
| A | GLN344 |
| A | 3PE2012 |
| B | ARG234 |
| C | TRP99 |
| C | LYS103 |
| C | TYR107 |
| C | VAL252 |
| C | VAL253 |
| C | PHE256 |
| C | 3PE2013 |
| C | HOH2043 |
| D | ALA34 |
| D | 3PE2011 |
| site_id | BC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 3PE D 2011 |
| Chain | Residue |
| A | LEU241 |
| A | VAL329 |
| A | GLN344 |
| A | TYR347 |
| A | 3PE2012 |
| C | TYR107 |
| C | PHE256 |
| C | ALA259 |
| C | 3PE2010 |
| D | ILE37 |
| D | LEU44 |
| D | ALA45 |
| D | ASN48 |
| D | ALA49 |
| D | HOH72 |
| site_id | BC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 3PE A 2012 |
| Chain | Residue |
| A | ARG216 |
| A | MET222 |
| A | TRP230 |
| A | TRP237 |
| A | VAL325 |
| C | VAL91 |
| C | 3PE2010 |
| D | THR22 |
| D | ALA33 |
| D | 3PE2011 |
| site_id | BC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 3PE C 2013 |
| Chain | Residue |
| C | ARG80 |
| C | ILE84 |
| C | HIS152 |
| C | TRP245 |
| C | HIS248 |
| C | 3PE2010 |
| C | HOH2035 |
| D | PHE23 |
| D | VAL30 |
| D | VAL35 |
| site_id | CC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE HEA G 1001 |
| Chain | Residue |
| G | GLY38 |
| G | THR48 |
| G | MET51 |
| G | ARG52 |
| G | TRP95 |
| G | ILE99 |
| G | HIS102 |
| G | GLY103 |
| G | MET106 |
| G | TRP172 |
| G | TYR414 |
| G | PHE420 |
| G | HIS421 |
| G | MET424 |
| G | SER425 |
| G | VAL429 |
| G | ILE432 |
| G | ILE436 |
| G | MET460 |
| G | THR467 |
| G | PHE468 |
| G | GLN471 |
| G | ARG481 |
| G | ARG482 |
| G | ALA501 |
| G | SER504 |
| G | PHE508 |
| G | HOH3022 |
| G | HOH3059 |
| site_id | CC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEA G 1002 |
| Chain | Residue |
| G | MET107 |
| G | TRP172 |
| G | TRP280 |
| G | VAL287 |
| G | TYR288 |
| G | VAL291 |
| G | HIS333 |
| G | HIS334 |
| G | GLY360 |
| G | PHE391 |
| G | GLY398 |
| G | LEU401 |
| G | SER402 |
| G | ASP407 |
| G | HIS411 |
| G | VAL416 |
| G | HIS419 |
| G | PHE420 |
| G | VAL423 |
| G | MET424 |
| G | ARG481 |
| G | HOH3018 |
| G | HOH3026 |
| G | HOH3052 |
| H | ILE68 |
| H | PRO108 |
| site_id | CC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 3PE I 3008 |
| Chain | Residue |
| I | LEU52 |
| I | MET55 |
| I | TRP59 |
| I | VAL62 |
| I | VAL63 |
| I | SER66 |
| I | LEU67 |
| I | HIS71 |
| I | PHE83 |
| I | PHE86 |
| I | PHE219 |
| I | ARG226 |
| I | HIS231 |
| I | PHE232 |
| I | HIS237 |
| I | VAL238 |
| I | GLY239 |
| I | HOH3041 |
| site_id | CC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 3PE G 3009 |
| Chain | Residue |
| G | PHE135 |
| G | PRO136 |
| G | ARG137 |
| G | MET138 |
| G | ILE202 |
| G | ALA247 |
| I | HIS10 |
| I | MET55 |
| I | TRP58 |
| I | TRP59 |
| I | GLY82 |
| I | PHE83 |
| I | PHE86 |
| site_id | CC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 3PE I 3010 |
| Chain | Residue |
| G | PHE281 |
| G | GLN344 |
| G | 3PE3012 |
| G | HOH3107 |
| H | ARG234 |
| I | TRP99 |
| I | LYS103 |
| I | TYR107 |
| I | VAL252 |
| I | VAL253 |
| I | PHE256 |
| I | 3PE3013 |
| J | ALA34 |
| J | 3PE3011 |
| site_id | CC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 3PE J 3011 |
| Chain | Residue |
| G | LEU241 |
| G | GLN344 |
| G | TYR347 |
| G | 3PE3012 |
| I | MET92 |
| I | TYR107 |
| I | PHE256 |
| I | ALA259 |
| I | 3PE3010 |
| J | ILE37 |
| J | LEU44 |
| J | ALA45 |
| J | ASN48 |
| J | ALA49 |
| site_id | CC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 3PE G 3012 |
| Chain | Residue |
| G | ARG216 |
| G | THR221 |
| G | MET222 |
| G | TRP230 |
| G | PHE233 |
| G | TRP237 |
| G | VAL325 |
| I | VAL91 |
| I | 3PE3010 |
| J | LYS21 |
| J | THR22 |
| J | MET29 |
| J | ALA33 |
| J | 3PE3011 |
| site_id | CC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 3PE I 3013 |
| Chain | Residue |
| I | ARG80 |
| I | ILE84 |
| I | ILE87 |
| I | HIS152 |
| I | TRP245 |
| I | HIS248 |
| I | 3PE3010 |
| I | HOH3036 |
| J | PHE23 |
| J | VAL30 |
| J | VAL35 |
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. WFFGHPqVyiivlpafgivshviatfakkpifgylpmvyamvaigvlgfvvwa..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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| B | PHE60-VAL80 | |
| A | PHE420-ILE440 | |
| A | LEU455-GLY475 | |
| A | LEU499-LEU519 | |
| G | ILE29-VAL49 | |
| G | VAL97-GLY117 | |
| G | LEU141-GLY161 | |
| G | LEU189-ILE209 | |
| G | LEU227-ALA247 | |
| G | ILE278-VAL298 | |
| G | ILE310-VAL330 | |
| B | TRP104-PHE124 | |
| G | PHE348-ALA368 | |
| G | MET381-LEU401 | |
| G | PHE420-ILE440 | |
| G | LEU455-GLY475 | |
| G | LEU499-LEU519 | |
| H | PHE60-VAL80 | |
| H | TRP104-PHE124 | |
| A | LEU227-ALA247 | |
| A | ILE278-VAL298 | |
| A | ILE310-VAL330 | |
| A | PHE348-ALA368 | |
| A | MET381-LEU401 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| B | HIS217 | |
| B | CYS252 | |
| B | CYS256 | |
| B | HIS260 | |
| H | HIS217 | |
| H | CYS252 | |
| H | CYS256 | |
| H | HIS260 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | HIS284 | |
| A | TYR288 | |
| A | HIS333 | |
| A | HIS334 | |
| G | HIS284 | |
| G | TYR288 | |
| G | HIS333 | |
| G | HIS334 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | CROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr) => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS284 | |
| A | TYR288 | |
| G | HIS284 | |
| G | TYR288 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1ar1 |
| Chain | Residue | Details |
| G | HIS419 | |
| G | HIS421 | |
| G | ARG482 | |
| G | ARG481 | |
| G | PHE420 | |
| G | TYR288 | |
| G | HIS284 |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1ar1 |
| Chain | Residue | Details |
| A | HIS419 | |
| A | HIS421 | |
| A | ARG482 | |
| A | ARG481 | |
| A | PHE420 | |
| A | TYR288 | |
| A | HIS284 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ar1 |
| Chain | Residue | Details |
| A | GLN286 | |
| A | LYS362 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ar1 |
| Chain | Residue | Details |
| G | GLN286 | |
| G | LYS362 |
