9F60
Structure of the Chlamydomonas reinhardtii respiratory complex IV from respiratory supercomplex
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 2A | 0004129 | molecular_function | cytochrome-c oxidase activity |
| 2A | 0005739 | cellular_component | mitochondrion |
| 2A | 0005743 | cellular_component | mitochondrial inner membrane |
| 2A | 0006119 | biological_process | oxidative phosphorylation |
| 2A | 0016020 | cellular_component | membrane |
| 2A | 0046872 | molecular_function | metal ion binding |
| 2A | 1902600 | biological_process | proton transmembrane transport |
| 2B | 0005739 | cellular_component | mitochondrion |
| 2B | 0016020 | cellular_component | membrane |
| 2B | 0016491 | molecular_function | oxidoreductase activity |
| 2B | 0031966 | cellular_component | mitochondrial membrane |
| 2B | 1902600 | biological_process | proton transmembrane transport |
| 2C | 0004129 | molecular_function | cytochrome-c oxidase activity |
| 2C | 0016020 | cellular_component | membrane |
| 2C | 0016491 | molecular_function | oxidoreductase activity |
| 2C | 0046872 | molecular_function | metal ion binding |
| 2C | 1902600 | biological_process | proton transmembrane transport |
| 2D | 0004129 | molecular_function | cytochrome-c oxidase activity |
| 2D | 0005739 | cellular_component | mitochondrion |
| 2D | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| 2D | 0016020 | cellular_component | membrane |
| 2D | 0016491 | molecular_function | oxidoreductase activity |
| 2D | 0045277 | cellular_component | respiratory chain complex IV |
| 2D | 1902600 | biological_process | proton transmembrane transport |
| 2E | 0005739 | cellular_component | mitochondrion |
| 2E | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| 2G | 0016020 | cellular_component | membrane |
| 2H | 0004129 | molecular_function | cytochrome-c oxidase activity |
| 2H | 0005739 | cellular_component | mitochondrion |
| 2H | 0016020 | cellular_component | membrane |
| 2H | 1902600 | biological_process | proton transmembrane transport |
| 2I | 0016020 | cellular_component | membrane |
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. WFFGHPeVyililpafgivsqvvsffsqkpvfgltgmicamgaisllgfivwa..HH |
| Chain | Residue | Details |
| 2A | TRP231-HIS285 |
| site_id | PS00078 |
| Number of Residues | 49 |
| Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VlHswavpalgvkmdavpgrlnqvwmsinregvfygq......CselCganHsfM |
| Chain | Residue | Details |
| 2C | VAL83-MET131 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 240 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| 2A | LEU14-ILE34 | |
| 2A | VAL374-ILE394 | |
| 2A | PHE408-ALA428 | |
| 2A | ALA446-PHE466 | |
| 2A | VAL55-GLY75 | |
| 2A | ASN98-GLU118 | |
| 2A | ALA143-VAL163 | |
| 2A | LEU180-ALA200 | |
| 2A | LEU229-VAL249 | |
| 2A | VAL261-VAL281 | |
| 2A | ALA302-TYR322 | |
| 2A | MET332-LEU352 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00401 |
| Chain | Residue | Details |
| 2A | GLU37 | |
| 2A | GLY42 | |
| 2A | HIS235 | |
| 2A | HIS284 | |
| 2A | HIS285 | |
| 2A | HIS362 | |
| 2A | ASP363 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: axial binding residue => ECO:0000250|UniProtKB:P00401 |
| Chain | Residue | Details |
| 2A | HIS60 | |
| 2A | HIS370 | |
| 2A | HIS372 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00396 |
| Chain | Residue | Details |
| 2A | TYR239 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | CROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr) => ECO:0000250|UniProtKB:P00401 |
| Chain | Residue | Details |
| 2A | HIS235 | |
| 2A | TYR239 |
