Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1KB9

YEAST CYTOCHROME BC1 COMPLEX

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
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM C 501
ChainResidue
CLEU40
CTHR127
CALA128
CGLY131
CVAL135
CHIS183
CTYR184
CPRO187
CHOH533
CHOH547
CGLN43
CGLY47
CILE48
CMET50
CALA51
CARG79
CHIS82
CPHE89
site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM C 502
ChainResidue
CTRP30
CGLY33
CLEU36
CHIS96
CLYS99
CSER105
CLEU113
CGLY117
CVAL118
CILE120
CHIS197
CLEU201
CSER206
CSER207
CUQ6506
CHOH515
CHOH534
site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM D 503
ChainResidue
DVAL100
DCYS101
DCYS104
DHIS105
DASN169
DPRO175
DARG184
DTYR190
DILE191
DPHE218
DILE223
DALA224
DMET225
DVAL228
DHOH513
site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES E 504
ChainResidue
ECYS159
EHIS161
ELEU162
ECYS178
EHIS181
ESER183
site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SMA C 505
ChainResidue
CILE125
CPHE129
CGLY143
CVAL146
CPRO271
CGLU272
CLEU275
CTYR279
CMET295
CPHE296
CHOH554
EHIS181
site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE UQ6 C 506
ChainResidue
CTYR16
CGLN22
CLEU40
CILE44
CLEU201
CSER206
CMET221
CASP229
CHEM502
site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PIE C 508
ChainResidue
CASN74
CMET237
CPHE245
DLEU269
DLYS272
DTHR273
DILE276
DHOH512
EGLY70
ESER73
EGLU76
ESER80
site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PEF C 510
ChainResidue
CALA98
CTYR102
CTYR103
CPHE326
CPHE327
CPHE329
CPHE333
GGLU82
HARG51
site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE CDL C 511
ChainResidue
CTYR28
CTRP29
CMET32
CMET95
CVAL231
CLEU235
CHOH565
CHOH612
DTYR281
DLYS288
DLYS289
DHOH553
GHIS85
CASN27
site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEF C 513
ChainResidue
CPHE3
CASN7
CVAL13
CTHR112
CASN115
CHOH605
site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PCF A 514
ChainResidue
ASER450
AUMQ521
CHIS222
EVAL60
ESER67
site_idBC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE UMQ A 521
ChainResidue
ATRP427
AASP428
ASER453
AMET454
AMET455
AARG456
APCF514
ETYR57
EVAL60
ESER68
IASN14
IALA15
IVAL16
IPHE17
IVAL18
IHOH439
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
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
ALYS74
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

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon