6JY3
Monomeric Form of Bovine Heart Cytochrome c Oxidase in the Fully Oxidized 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 | 26 |
Details | binding site for residue HEA A 601 |
Chain | Residue |
A | MET28 |
A | MET65 |
A | VAL70 |
A | GLY125 |
A | TRP126 |
A | TYR371 |
A | PHE377 |
A | HIS378 |
A | SER382 |
A | PHE393 |
A | MET417 |
A | THR31 |
A | PHE425 |
A | GLN428 |
A | ARG438 |
A | ARG439 |
A | HOH705 |
A | HOH716 |
A | HOH792 |
A | SER34 |
A | ILE37 |
A | ARG38 |
A | TYR54 |
A | VAL58 |
A | HIS61 |
A | ALA62 |
site_id | AC2 |
Number of Residues | 29 |
Details | binding site for residue HEA A 602 |
Chain | Residue |
A | TRP126 |
A | TRP236 |
A | VAL243 |
A | TYR244 |
A | HIS290 |
A | HIS291 |
A | THR309 |
A | ILE312 |
A | THR316 |
A | GLY317 |
A | GLY352 |
A | GLY355 |
A | ILE356 |
A | LEU358 |
A | ALA359 |
A | ASP364 |
A | HIS368 |
A | VAL373 |
A | HIS376 |
A | PHE377 |
A | VAL380 |
A | LEU381 |
A | ARG438 |
A | PER607 |
A | HOH710 |
A | HOH748 |
A | HOH800 |
A | HOH818 |
B | ILE34 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CU A 603 |
Chain | Residue |
A | HIS240 |
A | HIS290 |
A | HIS291 |
A | PER607 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG A 604 |
Chain | Residue |
A | HIS368 |
A | ASP369 |
B | GLU198 |
B | HOH403 |
B | HOH443 |
B | HOH505 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue NA A 605 |
Chain | Residue |
A | GLU40 |
A | GLY45 |
A | SER441 |
A | HOH844 |
site_id | AC6 |
Number of Residues | 13 |
Details | binding site for residue CDL A 606 |
Chain | Residue |
A | PHE2 |
A | ILE3 |
A | THR17 |
A | TRP25 |
A | LEU113 |
A | PHE400 |
L | PRO12 |
L | PHE13 |
L | SER14 |
L | ARG20 |
L | MET25 |
L | PHE28 |
L | PHE29 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue PER A 607 |
Chain | Residue |
A | HIS240 |
A | VAL243 |
A | HIS291 |
A | HEA602 |
A | CU603 |
site_id | AC8 |
Number of Residues | 18 |
Details | binding site for residue PGV A 608 |
Chain | Residue |
C | VAL61 |
C | GLU64 |
C | HIS71 |
C | GLY82 |
C | PEK303 |
G | CQX101 |
A | PHE94 |
A | PRO95 |
A | ARG96 |
A | MET97 |
A | HIS151 |
A | HOH802 |
A | HOH809 |
C | HIS9 |
C | ALA24 |
C | ASN50 |
C | TRP57 |
C | TRP58 |
site_id | AC9 |
Number of Residues | 10 |
Details | binding site for residue CQX A 609 |
Chain | Residue |
A | ASN406 |
A | THR408 |
A | TRP409 |
A | CQX611 |
A | HOH777 |
D | PHE87 |
D | HOH203 |
K | ASP8 |
K | PHE9 |
K | HIS10 |
site_id | AD1 |
Number of Residues | 15 |
Details | binding site for residue CQX A 610 |
Chain | Residue |
A | GLY49 |
A | ASP50 |
A | GLN52 |
A | ILE53 |
A | VAL56 |
A | ALA60 |
A | PHE109 |
A | LEU112 |
A | LEU113 |
A | SER116 |
A | ALA120 |
A | HOH701 |
A | HOH715 |
L | ILE39 |
L | GLN43 |
site_id | AD2 |
Number of Residues | 11 |
Details | binding site for residue CQX A 611 |
Chain | Residue |
A | SER478 |
A | ARG480 |
A | CQX609 |
A | HOH733 |
A | HOH854 |
K | PHE9 |
M | ALA6 |
M | PRO9 |
M | THR10 |
M | GLN15 |
M | HOH108 |
site_id | AD3 |
Number of Residues | 13 |
Details | binding site for residue CDL B 301 |
Chain | Residue |
A | PHE346 |
A | PHE426 |
A | HIS429 |
A | LEU433 |
A | HOH749 |
B | MET5 |
B | LEU7 |
B | GLY8 |
B | LEU28 |
B | SER35 |
B | HOH485 |
I | TYR35 |
I | ARG43 |
site_id | AD4 |
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 | AD5 |
Number of Residues | 9 |
Details | binding site for residue CQX B 303 |
Chain | Residue |
A | PHE321 |
A | HIS328 |
B | HIS52 |
B | MET56 |
B | GLU60 |
B | VAL61 |
B | TRP65 |
B | HOH409 |
B | HOH495 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue CQX B 304 |
Chain | Residue |
B | HIS26 |
B | MET29 |
B | HOH487 |
G | PHE21 |
G | PRO26 |
I | LYS36 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue CHD C 301 |
Chain | Residue |
A | HIS233 |
A | ASP300 |
A | THR301 |
A | TYR304 |
C | TRP99 |
C | HIS103 |
C | HOH450 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue NA C 302 |
Chain | Residue |
C | HIS148 |
C | HIS232 |
C | GLU236 |
site_id | AD9 |
Number of Residues | 20 |
Details | binding site for residue PEK C 303 |
Chain | Residue |
A | HIS151 |
A | VAL155 |
A | ALA203 |
A | PGV608 |
C | TRP34 |
C | TYR181 |
C | TYR182 |
C | ALA184 |
C | PHE186 |
C | THR187 |
C | ILE188 |
C | PHE198 |
C | GLY202 |
C | HOH441 |
G | THR68 |
G | PHE69 |
G | PHE70 |
G | HIS71 |
G | ASN76 |
G | HOH224 |
site_id | AE1 |
Number of Residues | 17 |
Details | binding site for residue PGV C 304 |
Chain | Residue |
C | VAL61 |
C | SER65 |
C | THR66 |
C | HIS207 |
C | PHE214 |
C | ARG221 |
C | HIS226 |
C | PHE227 |
C | THR228 |
C | HIS231 |
C | HIS232 |
C | PHE233 |
C | GLY234 |
C | HOH409 |
C | HOH430 |
C | HOH459 |
F | HOH210 |
site_id | AE2 |
Number of Residues | 12 |
Details | binding site for residue CDL C 305 |
Chain | Residue |
C | MET51 |
C | TYR55 |
C | ARG59 |
C | ILE62 |
C | ARG63 |
C | THR213 |
C | LYS224 |
C | HIS226 |
C | HOH414 |
J | LYS8 |
J | PHE12 |
J | THR27 |
site_id | AE3 |
Number of Residues | 9 |
Details | binding site for residue CQX C 306 |
Chain | Residue |
C | GLN177 |
C | TYR182 |
C | GLY205 |
C | CQX307 |
C | HOH402 |
G | PHE69 |
G | PHE70 |
G | HIS71 |
G | CQX101 |
site_id | AE4 |
Number of Residues | 7 |
Details | binding site for residue CQX C 307 |
Chain | Residue |
C | ALA178 |
C | SER179 |
C | TYR182 |
C | CQX306 |
C | HOH422 |
C | HOH427 |
G | PHE70 |
site_id | AE5 |
Number of Residues | 4 |
Details | binding site for residue ZN F 101 |
Chain | Residue |
F | CYS60 |
F | CYS62 |
F | CYS82 |
F | CYS85 |
site_id | AE6 |
Number of Residues | 7 |
Details | binding site for residue CQX G 101 |
Chain | Residue |
A | PGV608 |
C | TRP34 |
C | CQX306 |
G | TRP62 |
G | GLY63 |
G | PHE69 |
G | HOH206 |
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 |