Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4D6T

Cytochrome bc1 bound to the 4(1H)-pyridone GW844520

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0006627	biological_process	protein processing involved in protein targeting to mitochondrion
A	0016020	cellular_component	membrane
A	0017087	cellular_component	mitochondrial processing peptidase complex
A	0022904	biological_process	respiratory electron transport chain
A	0032991	cellular_component	protein-containing complex
A	0046872	molecular_function	metal ion binding
B	0004222	molecular_function	metalloendopeptidase activity
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0006508	biological_process	proteolysis
B	0022904	biological_process	respiratory electron transport chain
B	0045275	cellular_component	respiratory chain complex III
B	0046872	molecular_function	metal ion binding
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
C	0008121	molecular_function	quinol-cytochrome-c reductase activity
C	0009055	molecular_function	electron transfer activity
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0020037	molecular_function	heme binding
C	0022904	biological_process	respiratory electron transport chain
C	0031966	cellular_component	mitochondrial membrane
C	0045275	cellular_component	respiratory chain complex III
C	0046872	molecular_function	metal ion binding
C	0048039	molecular_function	ubiquinone binding
C	1902600	biological_process	proton transmembrane transport
D	0009055	molecular_function	electron transfer activity
D	0020037	molecular_function	heme binding
E	0005739	cellular_component	mitochondrion
E	0005743	cellular_component	mitochondrial inner membrane
E	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
E	0008121	molecular_function	quinol-cytochrome-c reductase activity
E	0016020	cellular_component	membrane
E	0016491	molecular_function	oxidoreductase activity
E	0022904	biological_process	respiratory electron transport chain
E	0031966	cellular_component	mitochondrial membrane
E	0045275	cellular_component	respiratory chain complex III
E	0046872	molecular_function	metal ion binding
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051537	molecular_function	2 iron, 2 sulfur cluster binding
E	1902600	biological_process	proton transmembrane transport
F	0005743	cellular_component	mitochondrial inner membrane
F	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
F	0016020	cellular_component	membrane
F	0022904	biological_process	respiratory electron transport chain
F	0045275	cellular_component	respiratory chain complex III
G	0005739	cellular_component	mitochondrion
G	0005743	cellular_component	mitochondrial inner membrane
G	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
G	0016020	cellular_component	membrane
G	0021539	biological_process	subthalamus development
G	0021548	biological_process	pons development
G	0021680	biological_process	cerebellar Purkinje cell layer development
G	0021766	biological_process	hippocampus development
G	0021794	biological_process	thalamus development
G	0021854	biological_process	hypothalamus development
G	0021860	biological_process	pyramidal neuron development
G	0022904	biological_process	respiratory electron transport chain
G	0030901	biological_process	midbrain development
G	0045275	cellular_component	respiratory chain complex III
H	0005743	cellular_component	mitochondrial inner membrane
H	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
H	0016020	cellular_component	membrane
H	0022904	biological_process	respiratory electron transport chain
H	0045275	cellular_component	respiratory chain complex III
H	0098803	cellular_component	respiratory chain complex
I	0005739	cellular_component	mitochondrion
I	0005743	cellular_component	mitochondrial inner membrane
I	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
I	0008121	molecular_function	quinol-cytochrome-c reductase activity
I	0016020	cellular_component	membrane
I	0016491	molecular_function	oxidoreductase activity
I	0022904	biological_process	respiratory electron transport chain
I	0031966	cellular_component	mitochondrial membrane
I	0045275	cellular_component	respiratory chain complex III
I	0046872	molecular_function	metal ion binding
I	0051536	molecular_function	iron-sulfur cluster binding
I	0051537	molecular_function	2 iron, 2 sulfur cluster binding
I	1902600	biological_process	proton transmembrane transport
J	0005739	cellular_component	mitochondrion
J	0005743	cellular_component	mitochondrial inner membrane
J	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
J	0016020	cellular_component	membrane
J	0022904	biological_process	respiratory electron transport chain
J	0045275	cellular_component	respiratory chain complex III
N	0005739	cellular_component	mitochondrion
N	0005743	cellular_component	mitochondrial inner membrane
N	0006627	biological_process	protein processing involved in protein targeting to mitochondrion
N	0016020	cellular_component	membrane
N	0017087	cellular_component	mitochondrial processing peptidase complex
N	0022904	biological_process	respiratory electron transport chain
N	0032991	cellular_component	protein-containing complex
N	0046872	molecular_function	metal ion binding
O	0004222	molecular_function	metalloendopeptidase activity
O	0005739	cellular_component	mitochondrion
O	0005743	cellular_component	mitochondrial inner membrane
O	0006508	biological_process	proteolysis
O	0022904	biological_process	respiratory electron transport chain
O	0045275	cellular_component	respiratory chain complex III
O	0046872	molecular_function	metal ion binding
P	0005739	cellular_component	mitochondrion
P	0005743	cellular_component	mitochondrial inner membrane
P	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
P	0008121	molecular_function	quinol-cytochrome-c reductase activity
P	0009055	molecular_function	electron transfer activity
P	0016020	cellular_component	membrane
P	0016491	molecular_function	oxidoreductase activity
P	0020037	molecular_function	heme binding
P	0022904	biological_process	respiratory electron transport chain
P	0031966	cellular_component	mitochondrial membrane
P	0045275	cellular_component	respiratory chain complex III
P	0046872	molecular_function	metal ion binding
P	0048039	molecular_function	ubiquinone binding
P	1902600	biological_process	proton transmembrane transport
Q	0009055	molecular_function	electron transfer activity
Q	0020037	molecular_function	heme binding
R	0005739	cellular_component	mitochondrion
R	0005743	cellular_component	mitochondrial inner membrane
R	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
R	0008121	molecular_function	quinol-cytochrome-c reductase activity
R	0016020	cellular_component	membrane
R	0016491	molecular_function	oxidoreductase activity
R	0022904	biological_process	respiratory electron transport chain
R	0031966	cellular_component	mitochondrial membrane
R	0045275	cellular_component	respiratory chain complex III
R	0046872	molecular_function	metal ion binding
R	0051536	molecular_function	iron-sulfur cluster binding
R	0051537	molecular_function	2 iron, 2 sulfur cluster binding
R	1902600	biological_process	proton transmembrane transport
S	0005743	cellular_component	mitochondrial inner membrane
S	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
S	0016020	cellular_component	membrane
S	0022904	biological_process	respiratory electron transport chain
S	0045275	cellular_component	respiratory chain complex III
T	0005739	cellular_component	mitochondrion
T	0005743	cellular_component	mitochondrial inner membrane
T	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
T	0016020	cellular_component	membrane
T	0021539	biological_process	subthalamus development
T	0021548	biological_process	pons development
T	0021680	biological_process	cerebellar Purkinje cell layer development
T	0021766	biological_process	hippocampus development
T	0021794	biological_process	thalamus development
T	0021854	biological_process	hypothalamus development
T	0021860	biological_process	pyramidal neuron development
T	0022904	biological_process	respiratory electron transport chain
T	0030901	biological_process	midbrain development
T	0045275	cellular_component	respiratory chain complex III
U	0005743	cellular_component	mitochondrial inner membrane
U	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
U	0016020	cellular_component	membrane
U	0022904	biological_process	respiratory electron transport chain
U	0045275	cellular_component	respiratory chain complex III
U	0098803	cellular_component	respiratory chain complex
V	0005739	cellular_component	mitochondrion
V	0005743	cellular_component	mitochondrial inner membrane
V	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
V	0008121	molecular_function	quinol-cytochrome-c reductase activity
V	0016020	cellular_component	membrane
V	0016491	molecular_function	oxidoreductase activity
V	0022904	biological_process	respiratory electron transport chain
V	0031966	cellular_component	mitochondrial membrane
V	0045275	cellular_component	respiratory chain complex III
V	0046872	molecular_function	metal ion binding
V	0051536	molecular_function	iron-sulfur cluster binding
V	0051537	molecular_function	2 iron, 2 sulfur cluster binding
V	1902600	biological_process	proton transmembrane transport
W	0005739	cellular_component	mitochondrion
W	0005743	cellular_component	mitochondrial inner membrane
W	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
W	0016020	cellular_component	membrane
W	0022904	biological_process	respiratory electron transport chain
W	0045275	cellular_component	respiratory chain complex III

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM C 501

Chain	Residue
C	LEU41
C	THR126
C	GLY130
C	TYR131
C	PRO134
C	HIS182
C	PHE183
C	PRO186
C	GLN44
C	ILE45
C	GLY48
C	LEU49
C	LEU51
C	ARG80
C	HIS83
C	ALA87

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM C 502

Chain	Residue
C	TRP31
C	GLY34
C	LEU37
C	HIS97
C	ARG100
C	SER106
C	TRP113
C	GLY116
C	HIS196
C	LEU200
C	SER205
C	ASN206
C	4X9503

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 4X9 C 503

Chain	Residue
C	PHE18
C	ILE27
C	SER35
C	GLY38
C	ILE42
C	MET190
C	MET194
C	HIS201
C	SER205
C	PHE220
C	ASP228
C	HEM502

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 C 504

Chain	Residue
A	SER439
C	HIS221

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PEE C 505

Chain	Residue
C	TRP30
C	TYR95
C	ARG100
C	TYR103
C	TYR104
C	MET316
C	TRP326
C	VAL329
C	LEU332
G	CDL501

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEC D 501

Chain	Residue
D	VAL36
D	CYS37
D	CYS40
D	HIS41
D	ASN105
D	PRO110
D	PRO111
D	ARG120
D	TYR126
D	PHE153
D	ILE158
D	GLY159
D	MET160
D	PRO163

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 D 502

Chain	Residue
D	PO4504
E	SER60

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PO4 D 503

Chain	Residue
D	ARG15

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 504

Chain	Residue
C	TYR75
D	PO4502
E	SER56
E	GLN57

site_id	BC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CDL D 505

Chain	Residue
C	SER29
C	ASN32
C	LYS227
C	LEU230
C	LEU234
D	TYR220
D	LYS223
D	ARG224
D	LYS231
F	ARG71
G	ASN36
G	CDL501

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEE D 506

Chain	Residue
D	HIS200
D	ARG203
D	MET204
D	LYS207
E	ASN53
E	VAL54
E	GLN57

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 E 501

Chain	Residue
A	PHE442
E	TYR37
E	THR40
J	PHE20

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 F 501

Chain	Residue
O	ARG134
O	TRP135
F	ARG49
F	TYR93

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CDL G 501

Chain	Residue
C	SER29
C	TRP30
C	PEE505
D	CDL505
F	GLN72
G	ARG40
G	THR41
G	CYS44

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 N 501

Chain	Residue
R	TYR37
R	THR40

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 N 1001

Chain	Residue
N	SER439
N	PHE442
P	HIS221

site_id	BC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM P 501

Chain	Residue
P	GLN44
P	GLY48
P	LEU49
P	LEU51
P	ARG80
P	HIS83
P	ALA84
P	PHE90
P	THR126
P	GLY130
P	TYR131
P	PRO134
P	HIS182
P	PHE183
P	PRO186

site_id	BC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM P 502

Chain	Residue
P	TRP31
P	GLY34
P	LEU37
P	PHE90
P	LEU94
P	HIS97
P	ARG100
P	SER106
P	PHE109
P	TRP113
P	GLY116
P	VAL117
P	LEU120
P	HIS196
P	LEU200
P	SER205
P	ASN206
P	4X9503

site_id	CC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 4X9 P 503

Chain	Residue
P	PHE18
P	TRP31
P	SER35
P	GLY38
P	LEU41
P	MET190
P	HIS201
P	SER205
P	PHE220
P	ASP228
P	HEM502

site_id	CC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PEE P 505

Chain	Residue
P	TRP30
P	TYR95
P	ARG100
P	LEU102
P	TYR103
P	TYR104
P	PHE276
P	MET316
P	TRP326
P	VAL329
S	GLN72
T	CDL501

site_id	CC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEC Q 501

Chain	Residue
Q	VAL36
Q	CYS37
Q	CYS40
Q	HIS41
Q	ASN105
Q	ARG120
Q	TYR126
Q	LEU131
Q	PHE153
Q	GLY159
Q	MET160
Q	PRO163

site_id	CC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CDL Q 505

Chain	Residue
P	SER29
P	LYS227
P	LEU235
Q	TYR220
Q	LYS223
Q	ARG224
Q	LYS231
S	ARG71
S	GLN72
T	ASN36
T	ARG40
T	CDL501

site_id	CC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PEE Q 506

Chain	Residue
P	LEU43
P	MET82
P	ILE236
Q	HIS200
Q	MET204
Q	LYS207
Q	MET211
Q	MET212
R	TYR49
R	ALA50
R	ASN53
R	GLN57
W	ASP36

site_id	CC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 Q 1001

Chain	Residue
Q	PO41002
R	SER60

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 Q 1002

Chain	Residue
Q	PO41001
R	SER56

site_id	CC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES R 501

Chain	Residue
R	CYS139
R	HIS141
R	LEU142
R	CYS144
R	CYS158
R	HIS161
R	SER163
R	PRO175

site_id	CC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL R 502

Chain	Residue
C	PHE168
R	ARG92
R	LYS94
R	ILE136

site_id	DC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 S 501

Chain	Residue
B	ARG134
S	TYR93

site_id	DC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CDL T 501

Chain	Residue
P	SER28
P	SER29
P	TRP30
P	MET96
P	PEE505
Q	CDL505
S	GLN72
T	VAL37
T	ARG40

Functional Information from PROSITE/UniProt

site_id	PS00143
Number of Residues	24
Details	INSULINASE Insulinase family, zinc-binding region signature. GsryensnnlGtSHLLRLAsSlTT

Chain	Residue	Details
O	GLY54-THR77
B	GLY54-THR77

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P31930","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CZ13","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CZ13","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q68FY0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DB77","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	322
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"1L0L","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	244
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	66
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	202
Details	Domain: {"description":"Cytochrome c","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	342
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	85
Details	Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BGY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D855","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D855","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CQ69","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P99028","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)