2YEV
Structure of caa3-type cytochrome oxidase
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 | 0006811 | biological_process | monoatomic ion transport |
| A | 0009055 | molecular_function | electron transfer activity |
| 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 | 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 | 0009055 | molecular_function | electron transfer activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0022900 | biological_process | electron transport chain |
| B | 0022904 | biological_process | respiratory 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 |
| D | 0004129 | molecular_function | cytochrome-c oxidase activity |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006119 | biological_process | oxidative phosphorylation |
| D | 0006811 | biological_process | monoatomic ion transport |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0009060 | biological_process | aerobic respiration |
| D | 0015990 | biological_process | electron transport coupled proton transport |
| D | 0016020 | cellular_component | membrane |
| D | 0020037 | molecular_function | heme binding |
| D | 0022904 | biological_process | respiratory electron transport chain |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1902600 | biological_process | proton transmembrane transport |
| E | 0004129 | molecular_function | cytochrome-c oxidase activity |
| E | 0005507 | molecular_function | copper ion binding |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0016020 | cellular_component | membrane |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0020037 | molecular_function | heme binding |
| E | 0022900 | biological_process | electron transport chain |
| E | 0022904 | biological_process | respiratory electron transport chain |
| E | 0042773 | biological_process | ATP synthesis coupled electron transport |
| E | 0046872 | molecular_function | metal ion binding |
| E | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE 5PL A 900 |
| Chain | Residue |
| A | LEU106 |
| A | GLU601 |
| A | ALA617 |
| A | PHE624 |
| A | LEU735 |
| A | ILE742 |
| A | PHE745 |
| A | GLN753 |
| A | LYS758 |
| A | THR766 |
| A | ALA769 |
| A | ARG108 |
| A | HOH2038 |
| A | HOH2136 |
| A | HOH2139 |
| A | HOH2154 |
| A | HOH2155 |
| A | VAL109 |
| A | PHE165 |
| A | PHE568 |
| A | LEU593 |
| A | TRP596 |
| A | ALA597 |
| A | ASP600 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE HAS A 1015 |
| Chain | Residue |
| A | PHE39 |
| A | ALA40 |
| A | GLY43 |
| A | SER46 |
| A | ILE49 |
| A | ARG50 |
| A | TYR66 |
| A | LEU70 |
| A | HIS73 |
| A | GLY74 |
| A | MET77 |
| A | LEU78 |
| A | GLY138 |
| A | TRP139 |
| A | TYR380 |
| A | PHE386 |
| A | HIS387 |
| A | LEU390 |
| A | MET391 |
| A | PHE434 |
| A | GLN437 |
| A | ARG447 |
| A | ARG448 |
| A | TYR449 |
| A | ALA470 |
| A | LEU473 |
| A | GLY474 |
| A | HOH2029 |
| A | HOH2111 |
| site_id | AC3 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE HAS A 1016 |
| Chain | Residue |
| A | TRP139 |
| A | TRP246 |
| A | VAL253 |
| A | TYR254 |
| A | HIS299 |
| A | HIS300 |
| A | THR318 |
| A | ILE321 |
| A | ALA322 |
| A | GLY326 |
| A | GLY361 |
| A | ILE362 |
| A | GLY364 |
| A | VAL365 |
| A | LEU367 |
| A | SER368 |
| A | ASP373 |
| A | HIS377 |
| A | VAL382 |
| A | HIS385 |
| A | PHE386 |
| A | VAL389 |
| A | LEU390 |
| A | SER394 |
| A | ARG447 |
| A | HOH2077 |
| A | HOH2091 |
| A | HOH2096 |
| A | HOH2100 |
| A | HOH2112 |
| B | PHE45 |
| B | SER46 |
| B | ILE49 |
| B | LEU98 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 1017 |
| Chain | Residue |
| A | HIS250 |
| A | HIS299 |
| A | HIS300 |
| A | HOH2076 |
| A | HOH2077 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 4AG A 1200 |
| Chain | Residue |
| B | ALA23 |
| B | THR25 |
| A | MET366 |
| A | ALA439 |
| A | TYR442 |
| A | LEU443 |
| A | ALA457 |
| A | TRP658 |
| B | ARG21 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 7E8 A 1300 |
| Chain | Residue |
| A | LEU29 |
| A | MET409 |
| A | THR410 |
| A | PRO511 |
| A | HOH2127 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE 7E8 A 1301 |
| Chain | Residue |
| A | GLN68 |
| A | PHE129 |
| A | HOH2032 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1801 |
| Chain | Residue |
| A | HIS377 |
| A | ASP378 |
| A | HOH2044 |
| A | HOH2101 |
| A | HOH2102 |
| B | GLU199 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CUA B 585 |
| Chain | Residue |
| B | HIS162 |
| B | CYS197 |
| B | GLU199 |
| B | CYS201 |
| B | HIS205 |
| B | MET208 |
| site_id | BC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEC B 587 |
| Chain | Residue |
| B | PHE126 |
| B | TRP127 |
| B | ASN141 |
| B | ASN246 |
| B | CYS247 |
| B | CYS250 |
| B | HIS251 |
| B | PRO264 |
| B | TRP269 |
| B | ARG272 |
| B | LEU275 |
| B | GLY276 |
| B | ALA277 |
| B | LEU287 |
| B | TRP290 |
| B | ILE291 |
| B | LYS298 |
| B | VAL301 |
| B | MET303 |
| B | PRO304 |
| B | LEU321 |
| B | HOH2018 |
| B | HOH2026 |
| B | HOH2069 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 7E9 B 701 |
| Chain | Residue |
| A | PHE665 |
| B | HOH2090 |
| D | LEU657 |
| D | TRP658 |
| D | LEU661 |
| D | LEU662 |
| D | PHE665 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL C 101 |
| Chain | Residue |
| A | THR308 |
| site_id | BC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE 5PL D 900 |
| Chain | Residue |
| D | LEU106 |
| D | ARG108 |
| D | PHE165 |
| D | LEU169 |
| D | ALA590 |
| D | LEU593 |
| D | TRP596 |
| D | ALA597 |
| D | ASP600 |
| D | GLU601 |
| D | GLU628 |
| D | LEU738 |
| D | ILE742 |
| D | PHE745 |
| D | GLY746 |
| D | GLN753 |
| D | LYS758 |
| D | GLY765 |
| D | THR766 |
| D | ALA769 |
| D | TYR773 |
| D | HOH2020 |
| D | HOH2093 |
| D | HOH2096 |
| D | HOH2111 |
| site_id | BC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HAS D 1015 |
| Chain | Residue |
| D | PHE37 |
| D | PHE39 |
| D | ALA40 |
| D | GLY43 |
| D | SER46 |
| D | ILE49 |
| D | ARG50 |
| D | TYR66 |
| D | LEU70 |
| D | HIS73 |
| D | MET77 |
| D | LEU78 |
| D | GLY138 |
| D | TRP139 |
| D | TYR380 |
| D | PHE386 |
| D | HIS387 |
| D | MET391 |
| D | PHE434 |
| D | GLN437 |
| D | ARG447 |
| D | ARG448 |
| D | TYR449 |
| D | LEU473 |
| D | HOH2012 |
| D | HOH2082 |
| site_id | BC6 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE HAS D 1016 |
| Chain | Residue |
| D | TRP139 |
| D | TRP246 |
| D | VAL253 |
| D | TYR254 |
| D | HIS299 |
| D | HIS300 |
| D | THR318 |
| D | ILE321 |
| D | ALA322 |
| D | GLY326 |
| D | LEU358 |
| D | GLY361 |
| D | ILE362 |
| D | GLY364 |
| D | VAL365 |
| D | LEU367 |
| D | SER368 |
| D | ASP373 |
| D | HIS377 |
| D | VAL382 |
| D | HIS385 |
| D | PHE386 |
| D | VAL389 |
| D | LEU390 |
| D | SER394 |
| D | ARG447 |
| D | HOH2054 |
| D | HOH2067 |
| D | HOH2074 |
| D | HOH2075 |
| D | HOH2083 |
| E | PHE45 |
| E | ILE49 |
| E | PRO91 |
| E | LEU98 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU D 1017 |
| Chain | Residue |
| D | HIS250 |
| D | HIS299 |
| D | HIS300 |
| D | HOH2053 |
| D | HOH2054 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 1701 |
| Chain | Residue |
| D | SER771 |
| D | HIS775 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 1801 |
| Chain | Residue |
| D | HIS377 |
| D | ASP378 |
| D | HOH2027 |
| D | HOH2070 |
| D | HOH2076 |
| E | GLU199 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CUA E 585 |
| Chain | Residue |
| E | HIS162 |
| E | CYS197 |
| E | GLU199 |
| E | CYS201 |
| E | HIS205 |
| E | MET208 |
| site_id | CC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEC E 587 |
| Chain | Residue |
| B | PRO307 |
| E | PHE126 |
| E | TRP127 |
| E | ASN141 |
| E | ASN246 |
| E | CYS247 |
| E | CYS250 |
| E | HIS251 |
| E | PRO264 |
| E | TRP269 |
| E | ARG272 |
| E | LEU275 |
| E | GLY276 |
| E | ALA277 |
| E | LEU287 |
| E | TRP290 |
| E | ILE291 |
| E | LYS298 |
| E | VAL301 |
| E | MET303 |
| E | PRO304 |
| E | PHE306 |
| E | LEU317 |
| E | HOH2004 |
| E | HOH2008 |
| E | HOH2030 |
| site_id | CC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL F 101 |
| Chain | Residue |
| D | THR308 |
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. WFYSHPtVyvmllpylgilaevastfarkplfgyrqmvwaqmgivvlgtmvwa..HH |
| Chain | Residue | Details |
| A | TRP246-HIS300 |
| site_id | PS00078 |
| Number of Residues | 49 |
| Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHsfwvpglagkrdaipgqttrisfepkepglyygf......CaelCgasHarM |
| Chain | Residue | Details |
| B | VAL160-MET208 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 720 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 492 |
| Details | Region: {"description":"COX3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
