7D5W
Bovine heart cytochrome c oxidase in a catalytic intermediate of O at 1.84 angstrom resolution
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 | 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 | 0045277 | cellular_component | respiratory chain complex IV |
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 | 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 | 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 | 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 | 0016020 | cellular_component | membrane |
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 | 0016020 | cellular_component | membrane |
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 |
N | 0004129 | molecular_function | cytochrome-c oxidase activity |
N | 0005739 | cellular_component | mitochondrion |
N | 0005743 | cellular_component | mitochondrial inner membrane |
N | 0006119 | biological_process | oxidative phosphorylation |
N | 0009060 | biological_process | aerobic respiration |
N | 0016020 | cellular_component | membrane |
N | 0020037 | molecular_function | heme binding |
N | 0022904 | biological_process | respiratory electron transport chain |
N | 0045277 | cellular_component | respiratory chain complex IV |
N | 0046872 | molecular_function | metal ion binding |
N | 1902600 | biological_process | proton transmembrane transport |
O | 0004129 | molecular_function | cytochrome-c oxidase activity |
O | 0005507 | molecular_function | copper ion binding |
O | 0005739 | cellular_component | mitochondrion |
O | 0005743 | cellular_component | mitochondrial inner membrane |
O | 0016020 | cellular_component | membrane |
O | 0016491 | molecular_function | oxidoreductase activity |
O | 0022900 | biological_process | electron transport chain |
O | 0031966 | cellular_component | mitochondrial membrane |
O | 0042773 | biological_process | ATP synthesis coupled electron transport |
O | 0045277 | cellular_component | respiratory chain complex IV |
O | 0046872 | molecular_function | metal ion binding |
O | 1902600 | biological_process | proton transmembrane transport |
P | 0004129 | molecular_function | cytochrome-c oxidase activity |
P | 0005739 | cellular_component | mitochondrion |
P | 0005743 | cellular_component | mitochondrial inner membrane |
P | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
P | 0008535 | biological_process | respiratory chain complex IV assembly |
P | 0009055 | molecular_function | electron transfer activity |
P | 0016020 | cellular_component | membrane |
P | 0019646 | biological_process | aerobic electron transport chain |
P | 0022904 | biological_process | respiratory electron transport chain |
P | 0045277 | cellular_component | respiratory chain complex IV |
P | 1902600 | biological_process | proton transmembrane transport |
Q | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
Q | 0045277 | cellular_component | respiratory chain complex IV |
R | 0005743 | cellular_component | mitochondrial inner membrane |
R | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
R | 0045277 | cellular_component | respiratory chain complex IV |
S | 0005740 | cellular_component | mitochondrial envelope |
S | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
S | 0045277 | cellular_component | respiratory chain complex IV |
T | 0005743 | cellular_component | mitochondrial inner membrane |
U | 0005739 | cellular_component | mitochondrion |
U | 0005743 | cellular_component | mitochondrial inner membrane |
U | 0006119 | biological_process | oxidative phosphorylation |
U | 0016020 | cellular_component | membrane |
U | 0045277 | cellular_component | respiratory chain complex IV |
V | 0005739 | cellular_component | mitochondrion |
V | 0005743 | cellular_component | mitochondrial inner membrane |
V | 0006119 | biological_process | oxidative phosphorylation |
V | 0016020 | cellular_component | membrane |
V | 0045277 | cellular_component | respiratory chain complex IV |
W | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
W | 0045277 | cellular_component | respiratory chain complex IV |
X | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
Y | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
Y | 0045277 | cellular_component | respiratory chain complex IV |
Z | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
Z | 0045277 | cellular_component | respiratory chain complex IV |
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 | 152 |
Details | Transmembrane: {"description":"Helical; Name=I","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 174 |
Details | Transmembrane: {"description":"Helical; Name=II","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 60 |
Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 108 |
Details | Transmembrane: {"description":"Helical; Name=III","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 94 |
Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 104 |
Details | Transmembrane: {"description":"Helical; Name=IV","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 112 |
Details | Transmembrane: {"description":"Helical; Name=V","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 130 |
Details | Transmembrane: {"description":"Helical; Name=VI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 78 |
Details | Transmembrane: {"description":"Helical; Name=VII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 56 |
Details | Transmembrane: {"description":"Helical; Name=VIII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 160 |
Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 42 |
Details | Transmembrane: {"description":"Helical; Name=IX","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 214 |
Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 58 |
Details | Transmembrane: {"description":"Helical; Name=X","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 52 |
Details | Transmembrane: {"description":"Helical; Name=XI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 62 |
Details | Transmembrane: {"description":"Helical; Name=XII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23537388","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI19 |
Number of Residues | 6 |
Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI20 |
Number of Residues | 22 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI22 |
Number of Residues | 4 |
Details | Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"PubMed","id":"10338009","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI23 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00406","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI24 |
Number of Residues | 384 |
Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI25 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI26 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P13073","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI27 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10888","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI28 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI29 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P12787","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI30 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P20674","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI31 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI32 |
Number of Residues | 6 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19536","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI33 |
Number of Residues | 92 |
Details | Domain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI34 |
Number of Residues | 20 |
Details | Motif: {"description":"Cx9C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI35 |
Number of Residues | 22 |
Details | Motif: {"description":"Cx10C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI36 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56391","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI37 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17665","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 14 |
Details | M-CSA 124 |
Chain | Residue | Details |
A | MET65 | metal ligand |
A | THR294 | metal ligand |
A | VAL295 | metal ligand, proton acceptor, proton donor |
A | VAL320 | proton acceptor, proton donor, proton relay |
A | TRP323 | proton acceptor, proton donor, proton relay |
A | ASP442 | proton acceptor, proton donor, proton relay |
A | PRO95 | proton acceptor, proton donor, proton relay |
A | PRO130 | proton acceptor, proton donor, proton relay |
A | GLY160 | proton acceptor, proton donor, proton relay |
A | ALA161 | proton acceptor, proton donor, proton relay |
A | TYR244 | covalently attached, electrostatic stabiliser, metal ligand, radical stabiliser |
A | LEU246 | proton acceptor, proton donor, proton relay |
A | LEU248 | covalently attached, hydrogen radical donor, proton acceptor, proton donor, proton relay, single electron acceptor |
A | THR259 | proton acceptor, proton donor, proton relay |
site_id | MCSA2 |
Number of Residues | 14 |
Details | M-CSA 124 |
Chain | Residue | Details |
N | MET65 | metal ligand |
N | THR294 | metal ligand |
N | VAL295 | metal ligand, proton acceptor, proton donor |
N | VAL320 | proton acceptor, proton donor, proton relay |
N | TRP323 | proton acceptor, proton donor, proton relay |
N | ASP442 | proton acceptor, proton donor, proton relay |
N | PRO95 | proton acceptor, proton donor, proton relay |
N | PRO130 | proton acceptor, proton donor, proton relay |
N | GLY160 | proton acceptor, proton donor, proton relay |
N | ALA161 | proton acceptor, proton donor, proton relay |
N | TYR244 | covalently attached, electrostatic stabiliser, metal ligand, radical stabiliser |
N | LEU246 | proton acceptor, proton donor, proton relay |
N | LEU248 | covalently attached, hydrogen radical donor, proton acceptor, proton donor, proton relay, single electron acceptor |
N | THR259 | proton acceptor, proton donor, proton relay |