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

8DH6

Cryo-EM structure of Saccharomyces cerevisiae cytochrome c oxidase (Complex IV) extracted in lipid nanodiscs

Functional Information from GO Data
ChainGOidnamespacecontents
a0004129molecular_functioncytochrome-c oxidase activity
a0005515molecular_functionprotein binding
a0005739cellular_componentmitochondrion
a0005743cellular_componentmitochondrial inner membrane
a0006119biological_processoxidative phosphorylation
a0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
a0009060biological_processaerobic respiration
a0016020cellular_componentmembrane
a0020037molecular_functionheme binding
a0022904biological_processrespiratory electron transport chain
a0031966cellular_componentmitochondrial membrane
a0045277cellular_componentrespiratory chain complex IV
a0045333biological_processcellular respiration
a0046872molecular_functionmetal ion binding
a1902600biological_processproton transmembrane transport
b0004129molecular_functioncytochrome-c oxidase activity
b0005507molecular_functioncopper ion binding
b0005515molecular_functionprotein binding
b0005739cellular_componentmitochondrion
b0005743cellular_componentmitochondrial inner membrane
b0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
b0009060biological_processaerobic respiration
b0016020cellular_componentmembrane
b0016491molecular_functionoxidoreductase activity
b0022900biological_processelectron transport chain
b0022904biological_processrespiratory electron 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
c0009055molecular_functionelectron transfer activity
c0009060biological_processaerobic respiration
c0016020cellular_componentmembrane
c0019646biological_processaerobic electron transport chain
c0022904biological_processrespiratory electron transport chain
c0031966cellular_componentmitochondrial membrane
c0045277cellular_componentrespiratory chain complex IV
c0045333biological_processcellular respiration
c0048039molecular_functionubiquinone binding
c1902600biological_processproton transmembrane transport
d0005740cellular_componentmitochondrial envelope
d0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
d0045277cellular_componentrespiratory chain complex IV
e0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
e0045277cellular_componentrespiratory chain complex IV
f0005743cellular_componentmitochondrial inner membrane
f0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
f0045277cellular_componentrespiratory chain complex IV
g0004129molecular_functioncytochrome-c oxidase activity
g0005739cellular_componentmitochondrion
g0005743cellular_componentmitochondrial inner membrane
g0006119biological_processoxidative phosphorylation
g0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
g0016491molecular_functionoxidoreductase activity
g0031966cellular_componentmitochondrial membrane
g0045277cellular_componentrespiratory chain complex IV
g0045333biological_processcellular respiration
g1902600biological_processproton transmembrane transport
h0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
h0045277cellular_componentrespiratory chain complex IV
i0004129molecular_functioncytochrome-c oxidase activity
i0005739cellular_componentmitochondrion
i0005743cellular_componentmitochondrial inner membrane
i0006119biological_processoxidative phosphorylation
i0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
i0016491molecular_functionoxidoreductase activity
i0045277cellular_componentrespiratory chain complex IV
i1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00848
Number of Residues23
DetailsCOX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. IMWlkptvnevarCweCGsvYKL
ChainResidueDetails
dILE121-LEU143
site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHdfaipslgikvdatpgrlnqvsaliqregvfyga......CselCgtgHanM
ChainResidueDetails
bVAL184-MET232
site_idPS00077
Number of Residues55
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyiliipgfgiishvvstyskkpvfgeismvyamasigllgflvws..HH
ChainResidueDetails
aTRP237-HIS291
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues290
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues75
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues337
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues86
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues53
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues51
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues54
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues62
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues41
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues29
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598556","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598556","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsCross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17215247","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17761666","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues101
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues3
DetailsPropeptide: {"featureId":"PRO_0000006174","evidences":[{"source":"PubMed","id":"6327685","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon