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5NMI

Cytochrome bc1 bound to the inhibitor MJM170

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0006627biological_processprotein processing involved in protein targeting to mitochondrion
A0016020cellular_componentmembrane
A0017087cellular_componentmitochondrial processing peptidase complex
A0022904biological_processrespiratory electron transport chain
A0032991cellular_componentprotein-containing complex
A0046872molecular_functionmetal ion binding
B0004222molecular_functionmetalloendopeptidase activity
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0006508biological_processproteolysis
B0022904biological_processrespiratory electron transport chain
B0045275cellular_componentrespiratory chain complex III
B0046872molecular_functionmetal ion binding
C0005739cellular_componentmitochondrion
C0005743cellular_componentmitochondrial inner membrane
C0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
C0008121molecular_functionquinol-cytochrome-c reductase activity
C0009055molecular_functionelectron transfer activity
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0020037molecular_functionheme binding
C0022904biological_processrespiratory electron transport chain
C0031966cellular_componentmitochondrial membrane
C0045275cellular_componentrespiratory chain complex III
C0046872molecular_functionmetal ion binding
C0048039molecular_functionubiquinone binding
C1902600biological_processproton transmembrane transport
D0009055molecular_functionelectron transfer activity
D0020037molecular_functionheme binding
E0005739cellular_componentmitochondrion
E0005743cellular_componentmitochondrial inner membrane
E0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
E0008121molecular_functionquinol-cytochrome-c reductase activity
E0016020cellular_componentmembrane
E0016491molecular_functionoxidoreductase activity
E0022904biological_processrespiratory electron transport chain
E0031966cellular_componentmitochondrial membrane
E0045275cellular_componentrespiratory chain complex III
E0046872molecular_functionmetal ion binding
E0051536molecular_functioniron-sulfur cluster binding
E0051537molecular_function2 iron, 2 sulfur cluster binding
E1902600biological_processproton transmembrane transport
F0005743cellular_componentmitochondrial inner membrane
F0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
F0016020cellular_componentmembrane
F0022904biological_processrespiratory electron transport chain
F0045275cellular_componentrespiratory chain complex III
G0005739cellular_componentmitochondrion
G0005743cellular_componentmitochondrial inner membrane
G0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
G0016020cellular_componentmembrane
G0021539biological_processsubthalamus development
G0021548biological_processpons development
G0021680biological_processcerebellar Purkinje cell layer development
G0021766biological_processhippocampus development
G0021794biological_processthalamus development
G0021854biological_processhypothalamus development
G0021860biological_processpyramidal neuron development
G0022904biological_processrespiratory electron transport chain
G0030901biological_processmidbrain development
G0045275cellular_componentrespiratory chain complex III
H0005743cellular_componentmitochondrial inner membrane
H0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
H0016020cellular_componentmembrane
H0022904biological_processrespiratory electron transport chain
H0045275cellular_componentrespiratory chain complex III
H0098803cellular_componentrespiratory chain complex
I0005739cellular_componentmitochondrion
I0005743cellular_componentmitochondrial inner membrane
I0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
I0008121molecular_functionquinol-cytochrome-c reductase activity
I0016020cellular_componentmembrane
I0016491molecular_functionoxidoreductase activity
I0022904biological_processrespiratory electron transport chain
I0031966cellular_componentmitochondrial membrane
I0045275cellular_componentrespiratory chain complex III
I0046872molecular_functionmetal ion binding
I0051536molecular_functioniron-sulfur cluster binding
I0051537molecular_function2 iron, 2 sulfur cluster binding
I1902600biological_processproton transmembrane transport
J0005739cellular_componentmitochondrion
J0005743cellular_componentmitochondrial inner membrane
J0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
J0016020cellular_componentmembrane
J0022904biological_processrespiratory electron transport chain
J0045275cellular_componentrespiratory chain complex III
K0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
N0005739cellular_componentmitochondrion
N0005743cellular_componentmitochondrial inner membrane
N0006627biological_processprotein processing involved in protein targeting to mitochondrion
N0016020cellular_componentmembrane
N0017087cellular_componentmitochondrial processing peptidase complex
N0022904biological_processrespiratory electron transport chain
N0032991cellular_componentprotein-containing complex
N0046872molecular_functionmetal ion binding
O0004222molecular_functionmetalloendopeptidase activity
O0005739cellular_componentmitochondrion
O0005743cellular_componentmitochondrial inner membrane
O0006508biological_processproteolysis
O0022904biological_processrespiratory electron transport chain
O0045275cellular_componentrespiratory chain complex III
O0046872molecular_functionmetal ion binding
P0005739cellular_componentmitochondrion
P0005743cellular_componentmitochondrial inner membrane
P0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
P0008121molecular_functionquinol-cytochrome-c reductase activity
P0009055molecular_functionelectron transfer activity
P0016020cellular_componentmembrane
P0016491molecular_functionoxidoreductase activity
P0020037molecular_functionheme binding
P0022904biological_processrespiratory electron transport chain
P0031966cellular_componentmitochondrial membrane
P0045275cellular_componentrespiratory chain complex III
P0046872molecular_functionmetal ion binding
P0048039molecular_functionubiquinone binding
P1902600biological_processproton transmembrane transport
Q0009055molecular_functionelectron transfer activity
Q0020037molecular_functionheme binding
R0005739cellular_componentmitochondrion
R0005743cellular_componentmitochondrial inner membrane
R0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
R0008121molecular_functionquinol-cytochrome-c reductase activity
R0016020cellular_componentmembrane
R0016491molecular_functionoxidoreductase activity
R0022904biological_processrespiratory electron transport chain
R0031966cellular_componentmitochondrial membrane
R0045275cellular_componentrespiratory chain complex III
R0046872molecular_functionmetal ion binding
R0051536molecular_functioniron-sulfur cluster binding
R0051537molecular_function2 iron, 2 sulfur cluster binding
R1902600biological_processproton transmembrane transport
S0005743cellular_componentmitochondrial inner membrane
S0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
S0016020cellular_componentmembrane
S0022904biological_processrespiratory electron transport chain
S0045275cellular_componentrespiratory chain complex III
T0005739cellular_componentmitochondrion
T0005743cellular_componentmitochondrial inner membrane
T0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
T0016020cellular_componentmembrane
T0021539biological_processsubthalamus development
T0021548biological_processpons development
T0021680biological_processcerebellar Purkinje cell layer development
T0021766biological_processhippocampus development
T0021794biological_processthalamus development
T0021854biological_processhypothalamus development
T0021860biological_processpyramidal neuron development
T0022904biological_processrespiratory electron transport chain
T0030901biological_processmidbrain development
T0045275cellular_componentrespiratory chain complex III
U0005743cellular_componentmitochondrial inner membrane
U0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
U0016020cellular_componentmembrane
U0022904biological_processrespiratory electron transport chain
U0045275cellular_componentrespiratory chain complex III
U0098803cellular_componentrespiratory chain complex
V0005739cellular_componentmitochondrion
V0005743cellular_componentmitochondrial inner membrane
V0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
V0008121molecular_functionquinol-cytochrome-c reductase activity
V0016020cellular_componentmembrane
V0016491molecular_functionoxidoreductase activity
V0022904biological_processrespiratory electron transport chain
V0031966cellular_componentmitochondrial membrane
V0045275cellular_componentrespiratory chain complex III
V0046872molecular_functionmetal ion binding
V0051536molecular_functioniron-sulfur cluster binding
V0051537molecular_function2 iron, 2 sulfur cluster binding
V1902600biological_processproton transmembrane transport
W0005739cellular_componentmitochondrion
W0005743cellular_componentmitochondrial inner membrane
W0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
W0016020cellular_componentmembrane
W0022904biological_processrespiratory electron transport chain
W0045275cellular_componentrespiratory chain complex III
X0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue HEM C 501
ChainResidue
CGLN44
CPHE179
CHIS182
CPHE183
CPRO186
CGLY48
CTYR55
CARG80
CHIS83
CTHR126
CGLY130
CLEU133
CPRO134

site_idAC2
Number of Residues17
Detailsbinding site for residue HEM C 502
ChainResidue
CTRP31
CGLY34
CLEU37
CPHE90
CLEU94
CHIS97
CVAL98
CARG100
CSER106
CTRP113
CGLY116
CVAL117
CHIS196
CLEU197
CLEU200
CASN206
CMJM503

site_idAC3
Number of Residues9
Detailsbinding site for residue MJM C 503
ChainResidue
CPHE18
CTRP31
CSER35
CILE39
CLEU197
CSER205
CPHE220
CASP228
CHEM502

site_idAC4
Number of Residues13
Detailsbinding site for residue PEE C 504
ChainResidue
CTRP30
CTYR95
CMET96
CTYR103
CTYR104
CMET316
CGLN322
CPHE325
CTRP326
CCDL506
FGLN72
GCYS44
GVAL48

site_idAC5
Number of Residues10
Detailsbinding site for residue CDL C 505
ChainResidue
APHE336
AARG436
ASER439
CMET11
CLYS12
CASN15
CASP20
CHIS221
CILE229
EPEE502

site_idAC6
Number of Residues7
Detailsbinding site for residue CDL C 506
ChainResidue
CSER28
CSER29
CTRP30
CPEE504
FGLN72
GARG40
GCYS44

site_idAC7
Number of Residues15
Detailsbinding site for residue HEC D 501
ChainResidue
DVAL32
DVAL36
DCYS37
DCYS40
DHIS41
DLEU109
DPRO110
DPRO111
DILE116
DARG120
DTYR126
DPHE153
DGLY159
DMET160
DPRO163

site_idAC8
Number of Residues13
Detailsbinding site for residue PEE D 502
ChainResidue
CLEU43
CILE236
DHIS200
DMET204
DLYS207
DMET211
DLEU215
ETYR49
EALA50
EASN53
EVAL54
EGLN57
JASP36

site_idAC9
Number of Residues16
Detailsbinding site for residue CDL D 503
ChainResidue
CMET89
CLYS227
CLEU230
CGLY231
DTYR220
DLYS223
DARG224
DLYS231
FMET70
GPRO27
GGLY33
GASN36
GVAL37
GARG40
CSER29
CASN32

site_idAD1
Number of Residues6
Detailsbinding site for residue FES E 501
ChainResidue
ECYS139
EHIS141
ELEU142
ECYS158
EHIS161
ESER163

site_idAD2
Number of Residues8
Detailsbinding site for residue PEE E 502
ChainResidue
APHE442
CCDL505
ETYR37
ETHR40
ETHR44
JARG15
JTHR17
JPHE20

site_idAD3
Number of Residues9
Detailsbinding site for residue CDL P 401
ChainResidue
PSER29
PASN32
PCDL407
QTYR220
QLYS223
QARG224
TGLY33
TASN36
TARG40

site_idAD4
Number of Residues15
Detailsbinding site for residue HEM P 402
ChainResidue
PGLN44
PILE45
PGLY48
PLEU49
PALA52
PTYR55
PARG80
PHIS83
PALA87
PGLY130
PLEU133
PPRO134
PHIS182
PPHE183
PPRO186

site_idAD5
Number of Residues17
Detailsbinding site for residue HEM P 403
ChainResidue
PTRP31
PGLY34
PLEU37
PPHE90
PLEU94
PHIS97
PVAL98
PARG100
PSER106
PGLY116
PVAL117
PHIS196
PLEU197
PLEU200
PSER205
PASN206
PMJM404

site_idAD6
Number of Residues7
Detailsbinding site for residue MJM P 404
ChainResidue
PPHE18
PILE27
PHIS201
PSER205
PPHE220
PASP228
PHEM403

site_idAD7
Number of Residues14
Detailsbinding site for residue PEE P 405
ChainResidue
PTRP30
PTYR95
PMET96
PTYR103
PTYR104
PMET316
PGLN322
PTRP326
PVAL329
PCDL407
SGLN72
TCYS44
TVAL48
TPHE52

site_idAD8
Number of Residues8
Detailsbinding site for residue CDL P 406
ChainResidue
NASP333
NARG436
NSER439
PASN15
PILE19
PHIS221
PILE229
RPEE202

site_idAD9
Number of Residues9
Detailsbinding site for residue CDL P 407
ChainResidue
PSER28
PSER29
PTRP30
PCDL401
PPEE405
SGLN72
TARG40
TTHR41
TCYS44

site_idAE1
Number of Residues10
Detailsbinding site for residue PEE R 201
ChainResidue
PLEU43
PMET240
QHIS200
QMET204
QLYS207
RTYR49
RALA50
RASN53
RVAL54
RGLN57

site_idAE2
Number of Residues6
Detailsbinding site for residue PEE R 202
ChainResidue
PCDL406
QMET222
RTYR37
RTHR40
WTHR17
WPHE20

site_idAE3
Number of Residues15
Detailsbinding site for Di-peptide HEC Q 501 and CYS Q 37
ChainResidue
QVAL32
QTYR33
QVAL36
QSER38
QSER39
QCYS40
QHIS41
QLEU109
QPRO111
QILE116
QARG120
QTYR126
QGLY159
QMET160
QPRO163

site_idAE4
Number of Residues14
Detailsbinding site for Di-peptide HEC Q 501 and CYS Q 40
ChainResidue
QVAL36
QCYS37
QSER38
QSER39
QHIS41
QPRO94
QLEU109
QPRO111
QILE116
QARG120
QTYR126
QGLY159
QMET160
QPRO163

site_idAE5
Number of Residues14
Detailsbinding site for Di-peptide HEC Q 501 and CYS Q 40
ChainResidue
QVAL36
QCYS37
QSER38
QSER39
QHIS41
QPRO94
QLEU109
QPRO111
QILE116
QARG120
QTYR126
QGLY159
QMET160
QPRO163

site_idAE6
Number of Residues15
Detailsbinding site for Di-peptide HEC Q 501 and CYS Q 37
ChainResidue
QVAL32
QTYR33
QVAL36
QSER38
QSER39
QCYS40
QHIS41
QLEU109
QPRO111
QILE116
QARG120
QTYR126
QGLY159
QMET160
QPRO163

Functional Information from PROSITE/UniProt
site_idPS00143
Number of Residues24
DetailsINSULINASE Insulinase family, zinc-binding region signature. GsryensnnlGtSHLLRLAsSlTT
ChainResidueDetails
BGLY54-THR77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P31930","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CZ13","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CZ13","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q68FY0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DB77","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues322
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"1L0L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00968","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12269811","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15312779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16024040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16924113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9204897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1L0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L0N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NU1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PPJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12269811","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15312779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16024040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16924113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9204897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BGY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L0N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PPJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12269811","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15312779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16024040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16924113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9204897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1L0N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NU1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PPJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15312779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16024040","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YBB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues244
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues103
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues202
DetailsDomain: {"description":"Cytochrome c","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues4
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BGY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BGY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues146
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues85
DetailsDomain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BGY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D855","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D855","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CQ69","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P99028","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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