Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7D5W

Bovine heart cytochrome c oxidase in a catalytic intermediate of O at 1.84 angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004129molecular_functioncytochrome-c oxidase activity
A0005743cellular_componentmitochondrial inner membrane
A0006119biological_processoxidative phosphorylation
A0009060biological_processaerobic respiration
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022904biological_processrespiratory electron transport chain
A0045277cellular_componentrespiratory chain complex IV
A0046872molecular_functionmetal ion binding
A1902600biological_processproton transmembrane transport
B0004129molecular_functioncytochrome-c oxidase activity
B0005507molecular_functioncopper ion binding
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0022900biological_processelectron transport chain
B0031966cellular_componentmitochondrial membrane
B0042773biological_processATP synthesis coupled electron transport
B0045277cellular_componentrespiratory chain complex IV
B0046872molecular_functionmetal ion binding
B1902600biological_processproton transmembrane transport
C0004129molecular_functioncytochrome-c oxidase activity
C0005739cellular_componentmitochondrion
C0005743cellular_componentmitochondrial inner membrane
C0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
C0008535biological_processrespiratory chain complex IV assembly
C0009055molecular_functionelectron transfer activity
C0016020cellular_componentmembrane
C0019646biological_processaerobic electron transport chain
C0022904biological_processrespiratory electron transport chain
C0045277cellular_componentrespiratory chain complex IV
C1902600biological_processproton transmembrane transport
D0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
D0045277cellular_componentrespiratory chain complex IV
E0005743cellular_componentmitochondrial inner membrane
E0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
E0045277cellular_componentrespiratory chain complex IV
F0005740cellular_componentmitochondrial envelope
F0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
F0045277cellular_componentrespiratory chain complex IV
G0005743cellular_componentmitochondrial inner membrane
H0005739cellular_componentmitochondrion
H0005743cellular_componentmitochondrial inner membrane
H0006119biological_processoxidative phosphorylation
H0016020cellular_componentmembrane
H0045277cellular_componentrespiratory chain complex IV
I0005743cellular_componentmitochondrial inner membrane
I0006119biological_processoxidative phosphorylation
I0016020cellular_componentmembrane
I0045277cellular_componentrespiratory chain complex IV
J0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
J0045277cellular_componentrespiratory chain complex IV
K0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
L0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
L0045277cellular_componentrespiratory chain complex IV
M0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
M0045277cellular_componentrespiratory chain complex IV
N0004129molecular_functioncytochrome-c oxidase activity
N0005743cellular_componentmitochondrial inner membrane
N0006119biological_processoxidative phosphorylation
N0009060biological_processaerobic respiration
N0016020cellular_componentmembrane
N0020037molecular_functionheme binding
N0022904biological_processrespiratory electron transport chain
N0045277cellular_componentrespiratory chain complex IV
N0046872molecular_functionmetal ion binding
N1902600biological_processproton transmembrane transport
O0004129molecular_functioncytochrome-c oxidase activity
O0005507molecular_functioncopper ion binding
O0005739cellular_componentmitochondrion
O0005743cellular_componentmitochondrial inner membrane
O0016020cellular_componentmembrane
O0016491molecular_functionoxidoreductase activity
O0022900biological_processelectron transport chain
O0031966cellular_componentmitochondrial membrane
O0042773biological_processATP synthesis coupled electron transport
O0045277cellular_componentrespiratory chain complex IV
O0046872molecular_functionmetal ion binding
O1902600biological_processproton transmembrane transport
P0004129molecular_functioncytochrome-c oxidase activity
P0005739cellular_componentmitochondrion
P0005743cellular_componentmitochondrial inner membrane
P0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
P0008535biological_processrespiratory chain complex IV assembly
P0009055molecular_functionelectron transfer activity
P0016020cellular_componentmembrane
P0019646biological_processaerobic electron transport chain
P0022904biological_processrespiratory electron transport chain
P0045277cellular_componentrespiratory chain complex IV
P1902600biological_processproton transmembrane transport
Q0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
Q0045277cellular_componentrespiratory chain complex IV
R0005743cellular_componentmitochondrial inner membrane
R0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
R0045277cellular_componentrespiratory chain complex IV
S0005740cellular_componentmitochondrial envelope
S0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
S0045277cellular_componentrespiratory chain complex IV
T0005743cellular_componentmitochondrial inner membrane
U0005739cellular_componentmitochondrion
U0005743cellular_componentmitochondrial inner membrane
U0006119biological_processoxidative phosphorylation
U0016020cellular_componentmembrane
U0045277cellular_componentrespiratory chain complex IV
V0005743cellular_componentmitochondrial inner membrane
V0006119biological_processoxidative phosphorylation
V0016020cellular_componentmembrane
V0045277cellular_componentrespiratory chain complex IV
W0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
W0045277cellular_componentrespiratory chain complex IV
X0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
Y0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
Y0045277cellular_componentrespiratory chain complex IV
Z0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
Z0045277cellular_componentrespiratory chain complex IV
Functional Information from PROSITE/UniProt
site_idPS00077
Number of Residues56
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyililpgfgmishivtyysgkkepfgymgmvwammsigflgfivwa.HH
ChainResidueDetails
ATRP236-HIS291
site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VlHswavpslglktdaipgrlnqttlmssrpglyygq......CseiCgsnHsfM
ChainResidueDetails
BVAL159-MET207
site_idPS00848
Number of Residues23
DetailsCOX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. VIWfwlhkgeaqrCpsCGthYKL
ChainResidueDetails
FVAL69-LEU91
site_idPS01329
Number of Residues18
DetailsCOX6A Cytochrome c oxidase subunit VIa signature. IRtKpFsWGDGnHTfFhN
ChainResidueDetails
GILE55-ASN72
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues152
DetailsTransmembrane: {"description":"Helical; Name=I","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues18
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues174
DetailsTransmembrane: {"description":"Helical; Name=II","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues60
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues108
DetailsTransmembrane: {"description":"Helical; Name=III","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues94
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues104
DetailsTransmembrane: {"description":"Helical; Name=IV","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues112
DetailsTransmembrane: {"description":"Helical; Name=V","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues130
DetailsTransmembrane: {"description":"Helical; Name=VI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues78
DetailsTransmembrane: {"description":"Helical; Name=VII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues56
DetailsTransmembrane: {"description":"Helical; Name=VIII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues160
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=IX","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues214
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues58
DetailsTransmembrane: {"description":"Helical; Name=X","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues52
DetailsTransmembrane: {"description":"Helical; Name=XI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues62
DetailsTransmembrane: {"description":"Helical; Name=XII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23537388","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues6
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues4
DetailsCross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"PubMed","id":"10338009","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues384
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P13073","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10888","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P12787","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P20674","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19536","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues92
DetailsDomain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues20
DetailsMotif: {"description":"Cx9C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues22
DetailsMotif: {"description":"Cx10C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56391","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17665","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues14
DetailsM-CSA 124
ChainResidueDetails
AMET65metal ligand
ATHR294metal ligand
AVAL295metal ligand, proton acceptor, proton donor
AVAL320proton acceptor, proton donor, proton relay
ATRP323proton acceptor, proton donor, proton relay
AASP442proton acceptor, proton donor, proton relay
APRO95proton acceptor, proton donor, proton relay
APRO130proton acceptor, proton donor, proton relay
AGLY160proton acceptor, proton donor, proton relay
AALA161proton acceptor, proton donor, proton relay
ATYR244covalently attached, electrostatic stabiliser, metal ligand, radical stabiliser
ALEU246proton acceptor, proton donor, proton relay
ALEU248covalently attached, hydrogen radical donor, proton acceptor, proton donor, proton relay, single electron acceptor
ATHR259proton acceptor, proton donor, proton relay
site_idMCSA2
Number of Residues14
DetailsM-CSA 124
ChainResidueDetails
NMET65metal ligand
NTHR294metal ligand
NVAL295metal ligand, proton acceptor, proton donor
NVAL320proton acceptor, proton donor, proton relay
NTRP323proton acceptor, proton donor, proton relay
NASP442proton acceptor, proton donor, proton relay
NPRO95proton acceptor, proton donor, proton relay
NPRO130proton acceptor, proton donor, proton relay
NGLY160proton acceptor, proton donor, proton relay
NALA161proton acceptor, proton donor, proton relay
NTYR244covalently attached, electrostatic stabiliser, metal ligand, radical stabiliser
NLEU246proton acceptor, proton donor, proton relay
NLEU248covalently attached, hydrogen radical donor, proton acceptor, proton donor, proton relay, single electron acceptor
NTHR259proton acceptor, proton donor, proton relay

243531

PDB entries from 2025-10-22

PDB statisticsPDBj update infoContact PDBjnumon