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3CX5

Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
A0006627biological_processprotein processing involved in protein targeting to mitochondrion
A0008121molecular_functionquinol-cytochrome-c reductase activity
A0009060biological_processaerobic respiration
A0016020cellular_componentmembrane
A0045275cellular_componentrespiratory chain complex III
A0045333biological_processcellular respiration
A0046872molecular_functionmetal ion binding
A1902600biological_processproton transmembrane transport
B0004222molecular_functionmetalloendopeptidase activity
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
B0006508biological_processproteolysis
B0008121molecular_functionquinol-cytochrome-c reductase activity
B0009060biological_processaerobic respiration
B0016020cellular_componentmembrane
B0030061cellular_componentmitochondrial crista
B0045275cellular_componentrespiratory chain complex III
B0045333biological_processcellular respiration
B0046872molecular_functionmetal ion binding
B1902600biological_processproton transmembrane transport
C0005739cellular_componentmitochondrion
C0005743cellular_componentmitochondrial inner membrane
C0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
C0008121molecular_functionquinol-cytochrome-c reductase activity
C0009055molecular_functionelectron transfer activity
C0009060biological_processaerobic respiration
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0022904biological_processrespiratory electron transport chain
C0045275cellular_componentrespiratory chain complex III
C0045333biological_processcellular respiration
C0046872molecular_functionmetal ion binding
C1902600biological_processproton transmembrane transport
D0009055molecular_functionelectron transfer activity
D0020037molecular_functionheme binding
E0008121molecular_functionquinol-cytochrome-c reductase activity
E0016020cellular_componentmembrane
E0051537molecular_function2 iron, 2 sulfur cluster binding
F0005739cellular_componentmitochondrion
F0005743cellular_componentmitochondrial inner membrane
F0005758cellular_componentmitochondrial intermembrane space
F0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
F0008121molecular_functionquinol-cytochrome-c reductase activity
F0009060biological_processaerobic respiration
F0016020cellular_componentmembrane
F0034399cellular_componentnuclear periphery
F0045275cellular_componentrespiratory chain complex III
F0045333biological_processcellular respiration
F1902600biological_processproton transmembrane transport
G0005739cellular_componentmitochondrion
G0005743cellular_componentmitochondrial inner membrane
G0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
G0008121molecular_functionquinol-cytochrome-c reductase activity
G0009060biological_processaerobic respiration
G0016020cellular_componentmembrane
G0034551biological_processmitochondrial respiratory chain complex III assembly
G0045275cellular_componentrespiratory chain complex III
G0045333biological_processcellular respiration
G0099617cellular_componentmatrix side of mitochondrial inner membrane
G1902600biological_processproton transmembrane transport
H0005739cellular_componentmitochondrion
H0005743cellular_componentmitochondrial inner membrane
H0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
H0008121molecular_functionquinol-cytochrome-c reductase activity
H0009060biological_processaerobic respiration
H0016020cellular_componentmembrane
H0045275cellular_componentrespiratory chain complex III
H0045333biological_processcellular respiration
H1902600biological_processproton transmembrane transport
I0005739cellular_componentmitochondrion
I0005743cellular_componentmitochondrial inner membrane
I0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
I0008121molecular_functionquinol-cytochrome-c reductase activity
I0009060biological_processaerobic respiration
I0016020cellular_componentmembrane
I0034551biological_processmitochondrial respiratory chain complex III assembly
I0045275cellular_componentrespiratory chain complex III
I0045333biological_processcellular respiration
I1902600biological_processproton transmembrane transport
L0004222molecular_functionmetalloendopeptidase activity
L0005515molecular_functionprotein binding
L0005739cellular_componentmitochondrion
L0005743cellular_componentmitochondrial inner membrane
L0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
L0006627biological_processprotein processing involved in protein targeting to mitochondrion
L0008121molecular_functionquinol-cytochrome-c reductase activity
L0009060biological_processaerobic respiration
L0016020cellular_componentmembrane
L0045275cellular_componentrespiratory chain complex III
L0045333biological_processcellular respiration
L0046872molecular_functionmetal ion binding
L1902600biological_processproton transmembrane transport
M0004222molecular_functionmetalloendopeptidase activity
M0005515molecular_functionprotein binding
M0005739cellular_componentmitochondrion
M0005743cellular_componentmitochondrial inner membrane
M0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
M0006508biological_processproteolysis
M0008121molecular_functionquinol-cytochrome-c reductase activity
M0009060biological_processaerobic respiration
M0016020cellular_componentmembrane
M0030061cellular_componentmitochondrial crista
M0045275cellular_componentrespiratory chain complex III
M0045333biological_processcellular respiration
M0046872molecular_functionmetal ion binding
M1902600biological_processproton transmembrane transport
N0005739cellular_componentmitochondrion
N0005743cellular_componentmitochondrial inner membrane
N0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
N0008121molecular_functionquinol-cytochrome-c reductase activity
N0009055molecular_functionelectron transfer activity
N0009060biological_processaerobic respiration
N0016020cellular_componentmembrane
N0016491molecular_functionoxidoreductase activity
N0022904biological_processrespiratory electron transport chain
N0045275cellular_componentrespiratory chain complex III
N0045333biological_processcellular respiration
N0046872molecular_functionmetal ion binding
N1902600biological_processproton transmembrane transport
O0009055molecular_functionelectron transfer activity
O0020037molecular_functionheme binding
P0008121molecular_functionquinol-cytochrome-c reductase activity
P0016020cellular_componentmembrane
P0051537molecular_function2 iron, 2 sulfur cluster binding
Q0005739cellular_componentmitochondrion
Q0005743cellular_componentmitochondrial inner membrane
Q0005758cellular_componentmitochondrial intermembrane space
Q0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
Q0008121molecular_functionquinol-cytochrome-c reductase activity
Q0009060biological_processaerobic respiration
Q0016020cellular_componentmembrane
Q0034399cellular_componentnuclear periphery
Q0045275cellular_componentrespiratory chain complex III
Q0045333biological_processcellular respiration
Q1902600biological_processproton transmembrane transport
R0005739cellular_componentmitochondrion
R0005743cellular_componentmitochondrial inner membrane
R0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
R0008121molecular_functionquinol-cytochrome-c reductase activity
R0009060biological_processaerobic respiration
R0016020cellular_componentmembrane
R0034551biological_processmitochondrial respiratory chain complex III assembly
R0045275cellular_componentrespiratory chain complex III
R0045333biological_processcellular respiration
R0099617cellular_componentmatrix side of mitochondrial inner membrane
R1902600biological_processproton transmembrane transport
S0005739cellular_componentmitochondrion
S0005743cellular_componentmitochondrial inner membrane
S0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
S0008121molecular_functionquinol-cytochrome-c reductase activity
S0009060biological_processaerobic respiration
S0016020cellular_componentmembrane
S0045275cellular_componentrespiratory chain complex III
S0045333biological_processcellular respiration
S1902600biological_processproton transmembrane transport
T0005739cellular_componentmitochondrion
T0005743cellular_componentmitochondrial inner membrane
T0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
T0008121molecular_functionquinol-cytochrome-c reductase activity
T0009060biological_processaerobic respiration
T0016020cellular_componentmembrane
T0034551biological_processmitochondrial respiratory chain complex III assembly
T0045275cellular_componentrespiratory chain complex III
T0045333biological_processcellular respiration
T1902600biological_processproton transmembrane transport
W0005515molecular_functionprotein binding
W0005739cellular_componentmitochondrion
W0005758cellular_componentmitochondrial intermembrane space
W0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
W0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
W0009055molecular_functionelectron transfer activity
W0020037molecular_functionheme binding
W0046872molecular_functionmetal ion binding
W1901612molecular_functioncardiolipin binding
Functional Information from PROSITE/UniProt
site_idPS00143
Number of Residues23
DetailsINSULINASE Insulinase family, zinc-binding region signature. Ggsryatkd.GvAHLLNRFnFqNT
ChainResidueDetails
BGLY37-THR59

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17761666","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues162
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8031140","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues366
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues208
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8031140","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KB9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P84","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IBZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PD4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues400
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9430684","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues234
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues24
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9430684","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues306
DetailsDomain: {"description":"Cytochrome c","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues74
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues18
DetailsCompositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues162
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues294
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues182
DetailsDomain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues6
DetailsRegion: {"description":"Hinge","evidences":[{"source":"PubMed","id":"30598556","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KB9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P84","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IBZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PD4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues20
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues2
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"N6,N6,N6-trimethyllysine; by CTM1","evidences":[{"source":"PubMed","id":"10791961","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"10821864","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hr6
ChainResidueDetails
ALYS74

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hr6
ChainResidueDetails
LLYS74

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hr6
ChainResidueDetails
BASN52

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hr6
ChainResidueDetails
MASN52

site_idMCSA1
Number of Residues1
DetailsM-CSA 208
ChainResidueDetails
EHIS181covalently attached, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser
CSER206electrostatic stabiliser, hydrogen bond donor, radical stabiliser
CLYS228electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser
CASP229electrostatic stabiliser, hydrogen bond acceptor, radical stabiliser
CGLU272hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser

site_idMCSA2
Number of Residues1
DetailsM-CSA 208
ChainResidueDetails
PHIS181covalently attached, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser
NSER206electrostatic stabiliser, hydrogen bond donor, radical stabiliser
NLYS228electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser
NASP229electrostatic stabiliser, hydrogen bond acceptor, radical stabiliser
NGLU272hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser

239492

PDB entries from 2025-07-30

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