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1OCO

BOVINE HEART CYTOCHROME C OXIDASE IN CARBON MONOXIDE-BOUND STATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004129molecular_functioncytochrome-c oxidase activity
A0005739cellular_componentmitochondrion
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
I0005739cellular_componentmitochondrion
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
N0005739cellular_componentmitochondrion
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
V0005739cellular_componentmitochondrion
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 PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 517
ChainResidue
ACMO520
AHIS240
AHIS290
AHIS291

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 518
ChainResidue
AHIS368
AASP369
BGLU198

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 519
ChainResidue
AGLU40
AGLN43
AGLY45
ASER441

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B 228
ChainResidue
BHIS161
BCYS196
BCYS200
BMET207
BCU229

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B 229
ChainResidue
BCYS196
BGLU198
BCYS200
BHIS204
BCU228

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 99
ChainResidue
FCYS60
FCYS62
FCYS82
FCYS85

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU N 517
ChainResidue
NHIS240
NHIS290
NHIS291
NCMO520

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG N 518
ChainResidue
NHIS368
NASP369
OGLU198

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA N 519
ChainResidue
NGLU40
NGLN43
NGLY45
NSER441

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU O 228
ChainResidue
OHIS161
OCYS196
OCYS200
OMET207
OCU229

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU O 229
ChainResidue
OCYS196
OGLU198
OCYS200
OHIS204
OCU228

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN S 99
ChainResidue
SCYS60
SCYS62
SCYS82
SCYS85

site_idBC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEA A 515
ChainResidue
AGLY27
ASER34
AILE37
AARG38
ATYR54
AHIS61
AALA62
AMET65
AVAL70
AGLY125
ATRP126
ATYR371
APHE377
AHIS378
ALEU381
ASER382
AVAL386
AMET390
APHE425
AGLN428
AARG438
AARG439
ATYR440
AMET468

site_idBC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEA A 516
ChainResidue
AARG438
ACMO520
BILE72
ATRP126
AVAL243
ATYR244
AHIS290
AHIS291
ATHR309
AILE312
AGLY317
AGLY352
AGLY355
AILE356
ALEU358
AALA359
AASP364
AHIS368
AHIS376
APHE377
AVAL380
ALEU381

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CMO A 520
ChainResidue
AHIS240
AHIS290
AHIS291
AHEA516
ACU517

site_idBC7
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEA N 515
ChainResidue
NGLY27
NSER34
NILE37
NARG38
NTYR54
NHIS61
NALA62
NMET65
NVAL70
NGLY125
NTRP126
NTYR371
NPHE377
NHIS378
NLEU381
NSER382
NMET390
NPHE425
NGLN428
NARG438
NARG439
NTYR440
NMET468

site_idBC8
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEA N 516
ChainResidue
NTRP126
NVAL243
NTYR244
NHIS290
NHIS291
NTHR309
NILE312
NTHR316
NGLY317
NGLY352
NGLY355
NILE356
NLEU358
NALA359
NASP364
NHIS368
NHIS376
NPHE377
NVAL380
NLEU381
NARG438
NCMO520
OILE72

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CMO N 520
ChainResidue
NHIS240
NVAL243
NHIS291
NHEA516
NCU517

site_idCXB
Number of Residues6
DetailsCARBON MONOXIDE BINDING SITE.
ChainResidue
AHEA516
ACU517
ACMO520
NHEA516
NCU517
NCMO520

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 Residues150
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues152
DetailsTransmembrane: {"description":"Helical; Name=I","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
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_FI4
Number of Residues174
DetailsTransmembrane: {"description":"Helical; Name=II","evidences":[{"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 Residues240
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 Residues558
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 Residues2
DetailsModified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues4
DetailsCross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"PubMed","id":"10338009","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues2
DetailsModified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"220175","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues384
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P13073","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10888","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P12787","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P20674","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI33
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_FI34
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19536","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI35
Number of Residues92
DetailsDomain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI36
Number of Residues20
DetailsMotif: {"description":"Cx9C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI37
Number of Residues22
DetailsMotif: {"description":"Cx10C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI38
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56391","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI39
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17665","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues7
DetailsAnnotated By Reference To The Literature 1ar1
ChainResidueDetails
NARG438
NPHE377
NARG439
NHIS376
NHIS240
NTYR244
NHIS378

site_idCSA2
Number of Residues7
DetailsAnnotated By Reference To The Literature 1ar1
ChainResidueDetails
AARG438
APHE377
AARG439
AHIS376
AHIS240
ATYR244
AHIS378

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ar1
ChainResidueDetails
AGLU242
ALYS319

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ar1
ChainResidueDetails
NGLU242
NLYS319

site_idMCSA1
Number of Residues14
DetailsM-CSA 124
ChainResidueDetails
AHIS61metal ligand
AHIS290metal ligand
AHIS291metal ligand, proton acceptor, proton donor
ATHR316proton acceptor, proton donor, proton relay
ALYS319proton acceptor, proton donor, proton relay
AARG438proton acceptor, proton donor, proton relay
AASP91proton acceptor, proton donor, proton relay
ATRP126proton acceptor, proton donor, proton relay
ASER156proton acceptor, proton donor, proton relay
ASER157proton acceptor, proton donor, proton relay
AHIS240covalently attached, electrostatic stabiliser, metal ligand, radical stabiliser
AGLU242proton acceptor, proton donor, proton relay
ATYR244covalently attached, hydrogen radical donor, proton acceptor, proton donor, proton relay, single electron acceptor
ASER255proton acceptor, proton donor, proton relay

site_idMCSA2
Number of Residues14
DetailsM-CSA 124
ChainResidueDetails
NHIS61metal ligand
NHIS290metal ligand
NHIS291metal ligand, proton acceptor, proton donor
NTHR316proton acceptor, proton donor, proton relay
NLYS319proton acceptor, proton donor, proton relay
NARG438proton acceptor, proton donor, proton relay
NASP91proton acceptor, proton donor, proton relay
NTRP126proton acceptor, proton donor, proton relay
NSER156proton acceptor, proton donor, proton relay
NSER157proton acceptor, proton donor, proton relay
NHIS240covalently attached, electrostatic stabiliser, metal ligand, radical stabiliser
NGLU242proton acceptor, proton donor, proton relay
NTYR244covalently attached, hydrogen radical donor, proton acceptor, proton donor, proton relay, single electron acceptor
NSER255proton acceptor, proton donor, proton relay

239492

PDB entries from 2025-07-30

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