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6YMY

Cytochrome c oxidase from Saccharomyces cerevisiae

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
i0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
j0004129molecular_functioncytochrome-c oxidase activity
j0005739cellular_componentmitochondrion
j0005743cellular_componentmitochondrial inner membrane
j0005758cellular_componentmitochondrial intermembrane space
j0006119biological_processoxidative phosphorylation
j0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
j0016491molecular_functionoxidoreductase activity
j0031966cellular_componentmitochondrial membrane
j0033617biological_processmitochondrial respiratory chain complex IV assembly
j0045277cellular_componentrespiratory chain complex IV
j0045333biological_processcellular respiration
j1902600biological_processproton transmembrane transport
k0005743cellular_componentmitochondrial inner membrane
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CU a 601
ChainResidue
aHIS241
aHIS290
aHIS291

site_idAC2
Number of Residues23
Detailsbinding site for residue HEA a 602
ChainResidue
aALA63
aMET66
aILE67
aTRP127
aTYR371
aVAL374
aPHE377
aHIS378
aLEU381
aSER382
aLEU389
aPHE390
aPHE425
aMET428
aARG438
aARG439
aALA461
aPHE19
aSER33
aILE36
aARG37
aVAL59
aHIS62

site_idAC3
Number of Residues20
Detailsbinding site for residue HEA a 603
ChainResidue
aTRP237
aVAL244
aTYR245
aHIS290
aHIS291
aILE312
aTHR316
aGLY317
aGLY352
aGLY355
aLEU358
aALA359
aASP364
aHIS368
aVAL373
aHIS376
aPHE377
aVAL380
aLEU381
aARG438

site_idAC4
Number of Residues4
Detailsbinding site for residue PTY a 604
ChainResidue
aHIS328
aLEU339
bMET57
eILE95

site_idAC5
Number of Residues10
Detailsbinding site for residue PTY a 605
ChainResidue
aPHE95
aPRO96
aARG97
aILE98
cHIS15
cSER62
cTRP65
cGLU72
cHIS79
cPHE94

site_idAC6
Number of Residues8
Detailsbinding site for residue CN3 a 606
ChainResidue
aASN406
aLYS408
aPHE466
aTYR470
aLYS487
ePHE94
eLYS97
hPHE54

site_idAC7
Number of Residues6
Detailsbinding site for residue CUA b 301
ChainResidue
bHIS186
bCYS221
bGLU223
bCYS225
bHIS229
bMET232

site_idAC8
Number of Residues4
Detailsbinding site for residue PTY b 302
ChainResidue
aPHE268
bGLY78
bTHR80
iLYS11

site_idAC9
Number of Residues15
Detailsbinding site for residue PTY b 303
ChainResidue
aTHR354
aPHE426
aPHE430
bTHR19
bPRO20
bTYR21
bALA22
bCYS23
iTRP32
iPHE36
iPTY101
mLEU51
mPRO54
mGLY55
mTYR58

site_idAD1
Number of Residues10
Detailsbinding site for residue PTY c 301
ChainResidue
cLEU235
cHIS239
cVAL241
cGLY242
cPHE66
cILE69
cALA73
cTHR74
cARG229
cHIS234

site_idAD2
Number of Residues16
Detailsbinding site for residue PCF c 302
ChainResidue
aSER204
aTHR208
aPHE216
cTYR189
cALA192
cALA193
cPHE194
cILE196
cTYR206
cGLY210
kTRP108
kTHR114
kLEU115
kPHE116
kTRP117
kASN122

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN d 201
ChainResidue
dCYS111
dHIS119
dCYS134
dCYS137

site_idAD4
Number of Residues2
Detailsbinding site for residue PTY e 201
ChainResidue
ePCF202
mPCF101

site_idAD5
Number of Residues6
Detailsbinding site for residue PCF e 202
ChainResidue
aTYR452
eALA111
eARG114
eGLY118
ePTY201
mPCF101

site_idAD6
Number of Residues3
Detailsbinding site for residue PTY i 101
ChainResidue
bPTY303
iTYR31
iPHE36

site_idAD7
Number of Residues7
Detailsbinding site for residue PCF m 101
ChainResidue
aILE456
bTYR21
ePTY201
ePCF202
mVAL57
mSER61
mALA63

Functional Information from PROSITE/UniProt
site_idPS00077
Number of Residues55
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyiliipgfgiishvvstyskkpvfgeismvyamasigllgflvws..HH
ChainResidueDetails
aTRP237-HIS291

site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHdfaipslgikvdatpgrlnqvsaliqregvfyga......CselCgtgHanM
ChainResidueDetails
bVAL184-MET232

site_idPS00848
Number of Residues23
DetailsCOX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. IMWlkptvnevarCweCGsvYKL
ChainResidueDetails
dILE121-LEU143

site_idPS01329
Number of Residues18
DetailsCOX6A Cytochrome c oxidase subunit VIa signature. IRsKpFfWGDGdKTlFwN
ChainResidueDetails
kILE101-ASN118

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues75
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues336
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues86
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues162
DetailsTopological domain: {"description":"Mitochondrial matrix","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 Residues128
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

site_idSWS_FT_FI25
Number of Residues43
DetailsDomain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues10
DetailsMotif: {"description":"Cx9C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues11
DetailsMotif: {"description":"Cx10C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17761666","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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