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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1EZV

STRUCTURE OF THE YEAST CYTOCHROME BC1 COMPLEX CO-CRYSTALLIZED WITH AN ANTIBODY FV-FRAGMENT

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
A0017087cellular_componentmitochondrial processing peptidase complex
A0022904biological_processrespiratory electron transport chain
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
B0022904biological_processrespiratory electron transport chain
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
F0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
F0008121molecular_functionquinol-cytochrome-c reductase activity
F0009060biological_processaerobic respiration
F0016020cellular_componentmembrane
F0022904biological_processrespiratory electron transport chain
F0034551biological_processmitochondrial respiratory chain complex III assembly
F0045275cellular_componentrespiratory chain complex III
F0045333biological_processcellular respiration
F0099617cellular_componentmatrix side of mitochondrial inner membrane
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
G0022904biological_processrespiratory electron transport chain
G0045275cellular_componentrespiratory chain complex III
G0045333biological_processcellular respiration
G1902600biological_processproton transmembrane transport
H0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
I0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
I0045275cellular_componentrespiratory chain complex III
X0002250biological_processadaptive immune response
X0002376biological_processimmune system process
X0003823molecular_functionantigen binding
X0005576cellular_componentextracellular region
X0005886cellular_componentplasma membrane
X0016064biological_processimmunoglobulin mediated immune response
X0019814cellular_componentimmunoglobulin complex
Y0002250biological_processadaptive immune response
Y0002376biological_processimmune system process
Y0005576cellular_componentextracellular region
Y0005886cellular_componentplasma membrane
Y0006955biological_processimmune response
Y0019814cellular_componentimmunoglobulin complex
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM C 401
ChainResidue
CLEU40
CPHE89
CTHR127
CALA128
CGLY131
CVAL135
CHIS183
CTYR184
CPRO187
CHOH527
CHOH539
CGLN43
CGLY47
CILE48
CMET50
CALA51
CARG79
CHIS82
CALA83
site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM C 402
ChainResidue
CTRP30
CGLY33
CLEU36
CHIS96
CLYS99
CSER105
CLEU113
CGLY117
CVAL118
CILE120
CHIS197
CLEU201
CSER206
CSER207
CUQ6506
CHOH508
CHOH528
site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEC D 3
ChainResidue
DVAL100
DCYS101
DCYS104
DHIS105
DASN169
DPRO175
DARG184
DTYR190
DILE191
DPHE218
DILE223
DALA224
DMET225
DVAL228
DHOH317
DHOH372
site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES E 4
ChainResidue
ECYS159
EHIS161
ELEU162
ECYS178
EHIS181
ESER183
site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SMA C 505
ChainResidue
CILE125
CPHE129
CVAL146
CILE269
CPRO271
CGLU272
CLEU275
CTYR279
CMET295
CPHE296
CHOH548
EHIS181
site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE UQ6 C 506
ChainResidue
CTYR16
CGLN22
CLEU40
CILE44
CPHE49
CMET52
CLEU198
CLEU201
CSER206
CMET221
CHEM402
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 Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17761666","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues81
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 Residues183
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 Residues104
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 Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
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 Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues200
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 Residues117
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 Residues153
DetailsDomain: {"description":"Cytochrome c","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues37
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues9
DetailsCompositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
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_FI15
Number of Residues1
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_FI16
Number of Residues1
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_FI17
Number of Residues66
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues147
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues91
DetailsDomain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues3
DetailsRegion: {"description":"Hinge","evidences":[{"source":"PubMed","id":"30598556","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues4
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_FI22
Number of Residues10
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues51
DetailsRegion: {"description":"Framework-1"}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues14
DetailsRegion: {"description":"Complementarity-determining-1"}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues27
DetailsRegion: {"description":"Framework-2"}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues22
DetailsRegion: {"description":"Complementarity-determining-2"}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues62
DetailsRegion: {"description":"Framework-3"}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues8
DetailsRegion: {"description":"Complementarity-determining-3"}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndo
ChainResidueDetails
EHIS181
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndo
ChainResidueDetails
ALYS73
site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndo
ChainResidueDetails
BASN52
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

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