6JY4
Monomeric Form of Bovine Heart Cytochrome c Oxidase in the Fully Reduced State
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004129 | molecular_function | cytochrome-c oxidase activity |
| 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 | 0015990 | biological_process | electron transport coupled proton transport |
| A | 0016020 | cellular_component | membrane |
| A | 0020037 | molecular_function | heme binding |
| A | 0045277 | cellular_component | respiratory chain complex IV |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004129 | molecular_function | cytochrome-c oxidase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0022900 | biological_process | electron transport chain |
| 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 | 0008535 | biological_process | respiratory chain complex IV assembly |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016020 | cellular_component | membrane |
| C | 0019646 | biological_process | aerobic electron transport chain |
| C | 0022904 | biological_process | respiratory electron transport chain |
| C | 0045277 | cellular_component | respiratory chain complex IV |
| C | 1902600 | biological_process | proton transmembrane transport |
| D | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| D | 0045277 | cellular_component | respiratory chain complex IV |
| E | 0005743 | cellular_component | mitochondrial inner membrane |
| E | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| E | 0045277 | cellular_component | respiratory chain complex IV |
| F | 0005740 | cellular_component | mitochondrial envelope |
| F | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| F | 0045277 | cellular_component | respiratory chain complex IV |
| G | 0005743 | cellular_component | mitochondrial inner membrane |
| H | 0005739 | cellular_component | mitochondrion |
| H | 0005743 | cellular_component | mitochondrial inner membrane |
| H | 0006119 | biological_process | oxidative phosphorylation |
| H | 0045277 | cellular_component | respiratory chain complex IV |
| I | 0005739 | cellular_component | mitochondrion |
| I | 0005743 | cellular_component | mitochondrial inner membrane |
| I | 0006119 | biological_process | oxidative phosphorylation |
| I | 0045277 | cellular_component | respiratory chain complex IV |
| J | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| J | 0045277 | cellular_component | respiratory chain complex IV |
| K | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| L | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| L | 0045277 | cellular_component | respiratory chain complex IV |
| M | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| M | 0045277 | cellular_component | respiratory chain complex IV |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue HEA A 601 |
| Chain | Residue |
| A | THR31 |
| A | VAL70 |
| A | ILE73 |
| A | GLY125 |
| A | TRP126 |
| A | TYR371 |
| A | PHE377 |
| A | HIS378 |
| A | SER382 |
| A | PHE393 |
| A | MET417 |
| A | SER34 |
| A | PHE425 |
| A | GLN428 |
| A | ARG438 |
| A | ARG439 |
| A | TYR440 |
| A | VAL465 |
| A | HOH711 |
| A | HOH713 |
| A | HOH738 |
| A | ILE37 |
| A | ARG38 |
| A | TYR54 |
| A | VAL58 |
| A | HIS61 |
| A | ALA62 |
| A | MET65 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | binding site for residue HEA A 602 |
| Chain | Residue |
| A | TRP126 |
| A | TRP236 |
| A | VAL243 |
| A | TYR244 |
| A | ILE247 |
| A | HIS290 |
| A | HIS291 |
| A | THR309 |
| A | ILE312 |
| A | THR316 |
| A | GLY317 |
| A | GLY352 |
| A | GLY355 |
| A | LEU358 |
| A | ALA359 |
| A | ASP364 |
| A | HIS368 |
| A | VAL373 |
| A | HIS376 |
| A | PHE377 |
| A | VAL380 |
| A | LEU381 |
| A | ARG438 |
| A | HOH725 |
| A | HOH729 |
| A | HOH787 |
| A | HOH816 |
| B | ILE34 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CU A 603 |
| Chain | Residue |
| A | HIS240 |
| A | HIS290 |
| A | HIS291 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 604 |
| Chain | Residue |
| A | HIS368 |
| A | ASP369 |
| B | GLU198 |
| B | HOH416 |
| B | HOH428 |
| B | HOH491 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 605 |
| Chain | Residue |
| A | GLU40 |
| A | GLY45 |
| A | SER441 |
| A | HOH793 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue CQX A 606 |
| Chain | Residue |
| A | PHE321 |
| A | HIS328 |
| A | HOH701 |
| A | HOH843 |
| B | HIS52 |
| B | MET56 |
| B | GLU60 |
| B | LEU68 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | binding site for residue PGV A 607 |
| Chain | Residue |
| A | PHE94 |
| A | PRO95 |
| A | ARG96 |
| A | MET97 |
| A | PHE148 |
| A | HIS151 |
| A | ILE158 |
| A | HOH764 |
| C | HIS9 |
| C | ALA24 |
| C | THR28 |
| C | ASN50 |
| C | TRP57 |
| C | TRP58 |
| C | GLU64 |
| C | HIS71 |
| C | GLY82 |
| C | HOH441 |
| G | PEK101 |
| G | CQX102 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue CQX A 608 |
| Chain | Residue |
| A | TRP409 |
| A | CQX609 |
| A | HOH737 |
| D | PHE87 |
| K | ASP8 |
| K | PHE9 |
| K | HIS10 |
| A | ASN406 |
| A | THR408 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue CQX A 609 |
| Chain | Residue |
| A | SER478 |
| A | ARG480 |
| A | CQX608 |
| D | PHE87 |
| K | PHE9 |
| M | ALA6 |
| M | PRO9 |
| M | THR10 |
| M | GLN15 |
| M | LEU19 |
| M | HOH104 |
| site_id | AD1 |
| Number of Residues | 13 |
| Details | binding site for residue CDL B 301 |
| Chain | Residue |
| A | LEU433 |
| B | MET5 |
| B | LEU7 |
| B | GLY8 |
| B | LEU28 |
| B | PHE32 |
| B | HOH410 |
| B | HOH479 |
| B | HOH494 |
| B | HOH500 |
| I | PHE31 |
| I | TYR35 |
| I | ARG43 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CUA B 302 |
| Chain | Residue |
| B | HIS161 |
| B | CYS196 |
| B | GLU198 |
| B | CYS200 |
| B | HIS204 |
| B | MET207 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue CQX B 303 |
| Chain | Residue |
| B | HIS26 |
| B | MET29 |
| G | PHE21 |
| I | LYS36 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue CHD C 301 |
| Chain | Residue |
| A | HIS233 |
| A | ASP300 |
| A | THR301 |
| A | TYR304 |
| A | HOH858 |
| C | TRP99 |
| C | HIS103 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue NA C 302 |
| Chain | Residue |
| C | HIS148 |
| C | HIS232 |
| C | GLU236 |
| site_id | AD6 |
| Number of Residues | 18 |
| Details | binding site for residue PGV C 303 |
| Chain | Residue |
| C | TRP58 |
| C | VAL61 |
| C | SER65 |
| C | THR66 |
| C | ILE210 |
| C | PHE214 |
| C | ARG221 |
| C | HIS226 |
| C | PHE227 |
| C | THR228 |
| C | HIS231 |
| C | HIS232 |
| C | PHE233 |
| C | GLY234 |
| C | HOH406 |
| C | HOH424 |
| C | HOH448 |
| F | HOH210 |
| site_id | AD7 |
| Number of Residues | 13 |
| Details | binding site for residue CDL C 304 |
| Chain | Residue |
| C | MET51 |
| C | TYR55 |
| C | ARG59 |
| C | ILE62 |
| C | ARG63 |
| C | THR213 |
| C | VAL217 |
| C | ARG221 |
| C | LYS224 |
| C | HIS226 |
| C | HOH411 |
| J | LYS8 |
| J | PHE12 |
| site_id | AD8 |
| Number of Residues | 9 |
| Details | binding site for residue CQX C 305 |
| Chain | Residue |
| C | GLN177 |
| C | TYR182 |
| C | GLY205 |
| C | CQX306 |
| C | HOH410 |
| G | PHE69 |
| G | PHE70 |
| G | HIS71 |
| G | CQX102 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue CQX C 306 |
| Chain | Residue |
| C | ALA178 |
| C | SER179 |
| C | TYR182 |
| C | CQX305 |
| C | HOH403 |
| G | PHE70 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN F 101 |
| Chain | Residue |
| F | CYS60 |
| F | CYS62 |
| F | CYS82 |
| F | CYS85 |
| site_id | AE2 |
| Number of Residues | 18 |
| Details | binding site for residue PEK G 101 |
| Chain | Residue |
| A | HIS151 |
| A | PGV607 |
| C | TRP34 |
| C | TYR181 |
| C | TYR182 |
| C | ALA184 |
| C | PHE186 |
| C | THR187 |
| C | ILE188 |
| C | PHE198 |
| C | GLY202 |
| G | THR68 |
| G | PHE69 |
| G | PHE70 |
| G | HIS71 |
| G | ASN76 |
| G | HOH205 |
| G | HOH226 |
| site_id | AE3 |
| Number of Residues | 7 |
| Details | binding site for residue CQX G 102 |
| Chain | Residue |
| A | PGV607 |
| C | TRP34 |
| C | CQX305 |
| G | TRP62 |
| G | GLY63 |
| G | PHE69 |
| G | HOH212 |
| site_id | AE4 |
| Number of Residues | 12 |
| Details | binding site for residue CDL L 101 |
| Chain | Residue |
| A | PHE2 |
| A | ILE3 |
| A | THR17 |
| A | LEU113 |
| A | PHE400 |
| L | ILE11 |
| L | PRO12 |
| L | PHE13 |
| L | SER14 |
| L | ARG20 |
| L | PHE28 |
| L | PHE29 |
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. WFFGHPeVyililpgfgmishivtyysgkkepfgymgmvwammsigflgfivwa.HH |
| Chain | Residue | Details |
| A | TRP236-HIS291 |
| site_id | PS00078 |
| Number of Residues | 49 |
| Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VlHswavpslglktdaipgrlnqttlmssrpglyygq......CseiCgsnHsfM |
| Chain | Residue | Details |
| B | VAL159-MET207 |
| site_id | PS00848 |
| Number of Residues | 23 |
| Details | COX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. VIWfwlhkgeaqrCpsCGthYKL |
| Chain | Residue | Details |
| F | VAL69-LEU91 |
| site_id | PS01329 |
| Number of Residues | 18 |
| Details | COX6A Cytochrome c oxidase subunit VIa signature. IRtKpFsWGDGnHTfFhN |
| Chain | Residue | Details |
| G | ILE55-ASN72 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | TOPO_DOM: Mitochondrial matrix => ECO:0000269|PubMed:27605664 |
| Chain | Residue | Details |
| M | ILE1-SER11 | |
| F | CYS62 | |
| F | CYS82 | |
| F | CYS85 | |
| A | SER401-ASN406 | |
| A | LYS479-LYS514 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 23 |
| Details | TRANSMEM: Helical => ECO:0000269|PubMed:27605664 |
| Chain | Residue | Details |
| M | PRO12-TYR35 | |
| F | LYS55 | |
| F | LYS90 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | TOPO_DOM: Mitochondrial intermembrane => ECO:0000269|PubMed:27605664 |
| Chain | Residue | Details |
| M | HIS36-ALA46 | |
| C | LEU106-GLU128 | |
| C | ALA184-ASP190 | |
| C | TYR257-SER261 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17665 |
| Chain | Residue | Details |
| L | LYS9 | |
| D | LYS38 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P13073 |
| Chain | Residue | Details |
| D | LYS31 | |
| B | CYS196 | |
| B | GLU198 | |
| B | CYS200 | |
| B | HIS204 | |
| B | MET207 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P10888 |
| Chain | Residue | Details |
| D | SER34 | |
| D | SER36 | |
| A | VAL287-ASP298 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P19783 |
| Chain | Residue | Details |
| D | LYS45 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 32 |
| Details | TRANSMEM: Helical; Name=VI => ECO:0000269|PubMed:27605664 |
| Chain | Residue | Details |
| C | GLY191-LEU223 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 23 |
| Details | TRANSMEM: Helical; Name=VII => ECO:0000269|PubMed:27605664 |
| Chain | Residue | Details |
| C | PHE233-ILE256 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 16 |
| Details | TRANSMEM: Helical; Name=VII => ECO:0000269|PubMed:27605664 |
| Chain | Residue | Details |
| A | TYR270-ILE286 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 28 |
| Details | TRANSMEM: Helical; Name=VIII => ECO:0000269|PubMed:27605664 |
| Chain | Residue | Details |
| A | VAL299-LEU327 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 7 |
| Details | TOPO_DOM: Mitochondrial matrix => ECO:0000269|PubMed:27605664 |
| Chain | Residue | Details |
| A | HIS328-SER335 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 21 |
| Details | TRANSMEM: Helical; Name=IX => ECO:0000269|PubMed:27605664 |
| Chain | Residue | Details |
| A | PRO336-VAL357 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 24 |
| Details | TOPO_DOM: Mitochondrial intermembrane => ECO:0000269|PubMed:27605664 |
| Chain | Residue | Details |
| A | LEU358-THR370 | |
| A | SER434-ALA446 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 29 |
| Details | TRANSMEM: Helical; Name=X => ECO:0000269|PubMed:27605664 |
| Chain | Residue | Details |
| A | TYR371-PHE400 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 26 |
| Details | TRANSMEM: Helical; Name=XI => ECO:0000269|PubMed:27605664 |
| Chain | Residue | Details |
| A | ASP407-LEU433 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 31 |
| Details | TRANSMEM: Helical; Name=XII => ECO:0000269|PubMed:27605664 |
| Chain | Residue | Details |
| A | TYR447-SER478 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27605664, ECO:0000305|PubMed:23537388 |
| Chain | Residue | Details |
| A | GLU40 | |
| A | GLY45 | |
| A | SER441 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 3 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158 |
| Chain | Residue | Details |
| A | HIS61 | |
| A | HIS376 | |
| A | HIS378 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158 |
| Chain | Residue | Details |
| A | HIS240 | |
| A | HIS290 | |
| A | HIS291 | |
| A | HIS368 | |
| A | ASP369 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | TYR244 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | MOD_RES: N-formylmethionine => ECO:0000269|PubMed:2165784 |
| Chain | Residue | Details |
| A | FME1 |
| site_id | SWS_FT_FI23 |
| Number of Residues | 2 |
| Details | CROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr) => ECO:0000269|PubMed:10338009 |
| Chain | Residue | Details |
| A | HIS240 | |
| A | TYR244 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 14 |
| Details | M-CSA 124 |
| Chain | Residue | Details |
| A | HIS61 | metal ligand |
| A | HIS290 | metal ligand |
| A | HIS291 | metal ligand, proton acceptor, proton donor |
| A | THR316 | proton acceptor, proton donor, proton relay |
| A | LYS319 | proton acceptor, proton donor, proton relay |
| A | ARG438 | proton acceptor, proton donor, proton relay |
| A | ASP91 | proton acceptor, proton donor, proton relay |
| A | TRP126 | proton acceptor, proton donor, proton relay |
| A | SER156 | proton acceptor, proton donor, proton relay |
| A | SER157 | proton acceptor, proton donor, proton relay |
| A | HIS240 | covalently attached, electrostatic stabiliser, metal ligand, radical stabiliser |
| A | GLU242 | proton acceptor, proton donor, proton relay |
| A | TYR244 | covalently attached, hydrogen radical donor, proton acceptor, proton donor, proton relay, single electron acceptor |
| A | SER255 | proton acceptor, proton donor, proton relay |
