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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8YHQ

Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in pyraclostrobin-bound state

This is a non-PDB format compatible entry.
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
F0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
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
I0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
I0045275cellular_componentrespiratory chain complex III
J0004222molecular_functionmetalloendopeptidase activity
J0005515molecular_functionprotein binding
J0005739cellular_componentmitochondrion
J0005743cellular_componentmitochondrial inner membrane
J0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
J0006627biological_processprotein processing involved in protein targeting to mitochondrion
J0008121molecular_functionquinol-cytochrome-c reductase activity
J0009060biological_processaerobic respiration
J0016020cellular_componentmembrane
J0045275cellular_componentrespiratory chain complex III
J0045333biological_processcellular respiration
J0046872molecular_functionmetal ion binding
J1902600biological_processproton transmembrane transport
K0004222molecular_functionmetalloendopeptidase activity
K0005515molecular_functionprotein binding
K0005739cellular_componentmitochondrion
K0005743cellular_componentmitochondrial inner membrane
K0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
K0006508biological_processproteolysis
K0008121molecular_functionquinol-cytochrome-c reductase activity
K0009060biological_processaerobic respiration
K0016020cellular_componentmembrane
K0030061cellular_componentmitochondrial crista
K0045275cellular_componentrespiratory chain complex III
K0045333biological_processcellular respiration
K0046872molecular_functionmetal ion binding
K1902600biological_processproton transmembrane transport
L0005739cellular_componentmitochondrion
L0005743cellular_componentmitochondrial inner membrane
L0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
L0008121molecular_functionquinol-cytochrome-c reductase activity
L0009055molecular_functionelectron transfer activity
L0009060biological_processaerobic respiration
L0016020cellular_componentmembrane
L0016491molecular_functionoxidoreductase activity
L0022904biological_processrespiratory electron transport chain
L0045275cellular_componentrespiratory chain complex III
L0045333biological_processcellular respiration
L0046872molecular_functionmetal ion binding
L1902600biological_processproton transmembrane transport
M0009055molecular_functionelectron transfer activity
M0020037molecular_functionheme binding
N0008121molecular_functionquinol-cytochrome-c reductase activity
N0016020cellular_componentmembrane
N0051537molecular_function2 iron, 2 sulfur cluster binding
O0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
P0005739cellular_componentmitochondrion
P0005743cellular_componentmitochondrial inner membrane
P0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
P0008121molecular_functionquinol-cytochrome-c reductase activity
P0009060biological_processaerobic respiration
P0016020cellular_componentmembrane
P0034551biological_processmitochondrial respiratory chain complex III assembly
P0045275cellular_componentrespiratory chain complex III
P0045333biological_processcellular respiration
P0099617cellular_componentmatrix side of mitochondrial inner membrane
P1902600biological_processproton transmembrane transport
Q0005739cellular_componentmitochondrion
Q0005743cellular_componentmitochondrial inner membrane
Q0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
Q0008121molecular_functionquinol-cytochrome-c reductase activity
Q0009060biological_processaerobic respiration
Q0016020cellular_componentmembrane
Q0045275cellular_componentrespiratory chain complex III
Q0045333biological_processcellular respiration
Q1902600biological_processproton transmembrane transport
R0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
R0045275cellular_componentrespiratory chain complex III
S0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
T0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
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_FI2
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 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_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
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_FI8
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_FI9
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17761666","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
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 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_FI19
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_FI20
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_FI21
Number of Residues132
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI22
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_FI23
Number of Residues182
DetailsDomain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues6
DetailsRegion: {"description":"Hinge","evidences":[{"source":"PubMed","id":"30598556","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
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_FI26
Number of Residues20
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues46
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 208
ChainResidueDetails
EHIS181covalently attached, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser
BLYS222electrostatic stabiliser, hydrogen bond donor, radical stabiliser
BPRO244electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser
BVAL245electrostatic stabiliser, hydrogen bond acceptor, radical stabiliser
BPHE288hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser
site_idMCSA2
Number of Residues1
DetailsM-CSA 208
ChainResidueDetails
NHIS181covalently attached, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser

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PDB entries from 2025-08-06

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