7Z10
Monomeric respiratory complex IV isolated from S. cerevisiae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| a | 0004129 | molecular_function | cytochrome-c oxidase activity |
| a | 0005515 | molecular_function | protein binding |
| a | 0005739 | cellular_component | mitochondrion |
| a | 0005743 | cellular_component | mitochondrial inner membrane |
| a | 0006119 | biological_process | oxidative phosphorylation |
| a | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| a | 0009060 | biological_process | aerobic respiration |
| a | 0016020 | cellular_component | membrane |
| a | 0020037 | molecular_function | heme binding |
| a | 0022904 | biological_process | respiratory electron transport chain |
| a | 0031966 | cellular_component | mitochondrial membrane |
| a | 0045277 | cellular_component | respiratory chain complex IV |
| a | 0045333 | biological_process | cellular respiration |
| 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 | 0005515 | molecular_function | protein binding |
| b | 0005739 | cellular_component | mitochondrion |
| b | 0005743 | cellular_component | mitochondrial inner membrane |
| b | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| b | 0009060 | biological_process | aerobic respiration |
| b | 0016020 | cellular_component | membrane |
| b | 0016491 | molecular_function | oxidoreductase activity |
| b | 0022900 | biological_process | electron transport chain |
| b | 0022904 | biological_process | respiratory electron transport chain |
| b | 0031966 | cellular_component | mitochondrial membrane |
| b | 0042773 | biological_process | ATP synthesis coupled electron transport |
| b | 0045277 | cellular_component | respiratory chain complex IV |
| b | 0046872 | molecular_function | metal ion binding |
| b | 1902600 | biological_process | proton transmembrane transport |
| c | 0004129 | molecular_function | cytochrome-c oxidase activity |
| c | 0005739 | cellular_component | mitochondrion |
| c | 0005743 | cellular_component | mitochondrial inner membrane |
| c | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| 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 | 0031966 | cellular_component | mitochondrial membrane |
| c | 0045277 | cellular_component | respiratory chain complex IV |
| c | 0045333 | biological_process | cellular respiration |
| c | 0048039 | molecular_function | ubiquinone binding |
| c | 1902600 | biological_process | proton transmembrane transport |
| d | 0005740 | cellular_component | mitochondrial envelope |
| d | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| d | 0045277 | cellular_component | respiratory chain complex IV |
| e | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| e | 0045277 | cellular_component | respiratory chain complex IV |
| f | 0005743 | cellular_component | mitochondrial inner membrane |
| f | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| f | 0045277 | cellular_component | respiratory chain complex IV |
| g | 0004129 | molecular_function | cytochrome-c oxidase activity |
| g | 0005739 | cellular_component | mitochondrion |
| g | 0005743 | cellular_component | mitochondrial inner membrane |
| g | 0006119 | biological_process | oxidative phosphorylation |
| g | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| g | 0016491 | molecular_function | oxidoreductase activity |
| g | 0031966 | cellular_component | mitochondrial membrane |
| g | 0045277 | cellular_component | respiratory chain complex IV |
| g | 0045333 | biological_process | cellular respiration |
| g | 1902600 | biological_process | proton transmembrane transport |
| h | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| h | 0045277 | cellular_component | respiratory chain complex IV |
| i | 0004129 | molecular_function | cytochrome-c oxidase activity |
| i | 0005739 | cellular_component | mitochondrion |
| i | 0005743 | cellular_component | mitochondrial inner membrane |
| i | 0006119 | biological_process | oxidative phosphorylation |
| i | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| i | 0016491 | molecular_function | oxidoreductase activity |
| i | 0045277 | cellular_component | respiratory chain complex IV |
| i | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue CU a 601 |
| Chain | Residue |
| a | HIS241 |
| a | HIS290 |
| a | HIS291 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | binding site for residue HEA a 602 |
| Chain | Residue |
| a | VAL59 |
| a | HIS62 |
| a | ALA63 |
| a | MET66 |
| a | TRP127 |
| a | TYR371 |
| a | PHE377 |
| a | HIS378 |
| a | LEU381 |
| a | SER382 |
| a | ILE386 |
| a | LEU389 |
| a | PHE390 |
| a | ILE424 |
| a | PHE425 |
| a | MET428 |
| a | ARG438 |
| a | ARG439 |
| a | ALA461 |
| a | LEU465 |
| a | PHE468 |
| a | PHE19 |
| a | ILE23 |
| a | GLY26 |
| a | THR30 |
| a | SER33 |
| a | ARG37 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | binding site for residue HEA a 603 |
| Chain | Residue |
| a | TRP127 |
| a | TRP237 |
| a | VAL244 |
| a | TYR245 |
| a | HIS290 |
| a | THR309 |
| a | THR316 |
| a | GLY317 |
| a | GLY352 |
| a | GLY355 |
| a | VAL356 |
| a | ALA359 |
| a | HIS368 |
| a | VAL373 |
| a | HIS376 |
| a | PHE377 |
| a | VAL380 |
| a | LEU381 |
| a | ARG438 |
| b | ILE50 |
| b | PRO89 |
| b | LEU93 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MG a 604 |
| Chain | Residue |
| a | HIS368 |
| a | ASP369 |
| b | GLU223 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue PEF a 605 |
| Chain | Residue |
| a | PHE95 |
| a | PRO96 |
| a | ARG97 |
| a | ILE98 |
| c | HIS15 |
| c | TRP65 |
| c | PHE66 |
| c | ILE69 |
| c | HIS79 |
| c | PHE94 |
| c | PEF301 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue PEF a 606 |
| Chain | Residue |
| a | LEU17 |
| a | PHE19 |
| a | MET20 |
| a | ILE400 |
| h | PRO39 |
| h | PHE40 |
| h | ARG45 |
| h | HIS53 |
| h | PHE56 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CUA b 301 |
| Chain | Residue |
| b | HIS186 |
| b | CYS221 |
| b | GLU223 |
| b | CYS225 |
| b | HIS229 |
| b | MET232 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | binding site for residue PEF c 301 |
| Chain | Residue |
| a | PEF605 |
| c | PHE66 |
| c | ILE69 |
| c | VAL70 |
| c | THR74 |
| c | ILE87 |
| c | PHE91 |
| c | MET222 |
| c | VAL225 |
| c | ARG229 |
| c | HIS234 |
| c | THR236 |
| c | HIS239 |
| c | VAL241 |
| c | GLY242 |
| d | GLU63 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN d 201 |
| Chain | Residue |
| d | CYS134 |
| d | CYS137 |
| d | CYS111 |
| d | HIS119 |
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. WFFGHPeVyiliipgfgiishvvstyskkpvfgeismvyamasigllgflvws..HH |
| Chain | Residue | Details |
| a | TRP237-HIS291 |
| site_id | PS00078 |
| Number of Residues | 49 |
| Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHdfaipslgikvdatpgrlnqvsaliqregvfyga......CselCgtgHanM |
| Chain | Residue | Details |
| b | VAL184-MET232 |
| site_id | PS00848 |
| Number of Residues | 23 |
| Details | COX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. IMWlkptvnevarCweCGsvYKL |
| Chain | Residue | Details |
| d | ILE121-LEU143 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 290 |
| Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 75 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 337 |
| Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 86 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 53 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 51 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 54 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 62 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 41 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 29 |
| Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598556","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598556","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17215247","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17761666","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 101 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






