Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5KLI

Rhodobacter sphaeroides bc1 with stigmatellin and antimycin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005886	cellular_component	plasma membrane
A	0008121	molecular_function	quinol-cytochrome-c reductase activity
A	0009055	molecular_function	electron transfer activity
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0022904	biological_process	respiratory electron transport chain
A	0045275	cellular_component	respiratory chain complex III
A	0046872	molecular_function	metal ion binding
A	1902600	biological_process	proton transmembrane transport
B	0005886	cellular_component	plasma membrane
B	0009055	molecular_function	electron transfer activity
B	0020037	molecular_function	heme binding
B	0022904	biological_process	respiratory electron transport chain
B	0046872	molecular_function	metal ion binding
C	0005886	cellular_component	plasma membrane
C	0008121	molecular_function	quinol-cytochrome-c reductase activity
C	0016020	cellular_component	membrane
C	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
C	1902600	biological_process	proton transmembrane transport
E	0005886	cellular_component	plasma membrane
E	0008121	molecular_function	quinol-cytochrome-c reductase activity
E	0009055	molecular_function	electron transfer activity
E	0016020	cellular_component	membrane
E	0016491	molecular_function	oxidoreductase activity
E	0022904	biological_process	respiratory electron transport chain
E	0045275	cellular_component	respiratory chain complex III
E	0046872	molecular_function	metal ion binding
E	1902600	biological_process	proton transmembrane transport
F	0005886	cellular_component	plasma membrane
F	0009055	molecular_function	electron transfer activity
F	0020037	molecular_function	heme binding
F	0022904	biological_process	respiratory electron transport chain
F	0046872	molecular_function	metal ion binding
G	0005886	cellular_component	plasma membrane
G	0008121	molecular_function	quinol-cytochrome-c reductase activity
G	0016020	cellular_component	membrane
G	0046872	molecular_function	metal ion binding
G	0051536	molecular_function	iron-sulfur cluster binding
G	0051537	molecular_function	2 iron, 2 sulfur cluster binding
G	1902600	biological_process	proton transmembrane transport
K	0005886	cellular_component	plasma membrane
K	0008121	molecular_function	quinol-cytochrome-c reductase activity
K	0009055	molecular_function	electron transfer activity
K	0016020	cellular_component	membrane
K	0016491	molecular_function	oxidoreductase activity
K	0022904	biological_process	respiratory electron transport chain
K	0045275	cellular_component	respiratory chain complex III
K	0046872	molecular_function	metal ion binding
K	1902600	biological_process	proton transmembrane transport
L	0005886	cellular_component	plasma membrane
L	0009055	molecular_function	electron transfer activity
L	0020037	molecular_function	heme binding
L	0022904	biological_process	respiratory electron transport chain
L	0046872	molecular_function	metal ion binding
M	0005886	cellular_component	plasma membrane
M	0008121	molecular_function	quinol-cytochrome-c reductase activity
M	0016020	cellular_component	membrane
M	0046872	molecular_function	metal ion binding
M	0051536	molecular_function	iron-sulfur cluster binding
M	0051537	molecular_function	2 iron, 2 sulfur cluster binding
M	1902600	biological_process	proton transmembrane transport
O	0005886	cellular_component	plasma membrane
O	0008121	molecular_function	quinol-cytochrome-c reductase activity
O	0009055	molecular_function	electron transfer activity
O	0016020	cellular_component	membrane
O	0016491	molecular_function	oxidoreductase activity
O	0022904	biological_process	respiratory electron transport chain
O	0045275	cellular_component	respiratory chain complex III
O	0046872	molecular_function	metal ion binding
O	1902600	biological_process	proton transmembrane transport
P	0005886	cellular_component	plasma membrane
P	0009055	molecular_function	electron transfer activity
P	0020037	molecular_function	heme binding
P	0022904	biological_process	respiratory electron transport chain
P	0046872	molecular_function	metal ion binding
Q	0005886	cellular_component	plasma membrane
Q	0008121	molecular_function	quinol-cytochrome-c reductase activity
Q	0016020	cellular_component	membrane
Q	0046872	molecular_function	metal ion binding
Q	0051536	molecular_function	iron-sulfur cluster binding
Q	0051537	molecular_function	2 iron, 2 sulfur cluster binding
Q	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue HEM A 1001

Chain	Residue
A	GLN58
A	TYR147
A	LEU149
A	PRO150
A	HIS198
A	TYR199
A	PRO202
A	TYR297
A	GLY62
A	ILE63
A	LEU65
A	ARG94
A	HIS97
A	ALA101
A	THR142
A	GLY146

site_id	AC2
Number of Residues	17
Details	binding site for residue HEM A 1002

Chain	Residue
A	TRP45
A	GLY48
A	LEU51
A	PHE104
A	HIS111
A	ARG114
A	SER120
A	ARG125
A	GLY132
A	MET133
A	ILE135
A	HIS212
A	PHE216
A	GLY220
A	ASN221
A	ASN222
A	ANJ1004

site_id	AC3
Number of Residues	15
Details	binding site for residue SMA A 1003

Chain	Residue
A	MET140
A	PHE144
A	MET145
A	MET154
A	GLY158
A	VAL161
A	ILE162
A	LEU197
A	PRO294
A	GLU295
A	PHE298
A	TYR302
A	MET336
A	PHE337
G	HIS152

site_id	AC4
Number of Residues	12
Details	binding site for residue ANJ A 1004

Chain	Residue
A	TRP45
A	VAL49
A	ALA52
A	ALA206
A	VAL209
A	ILE213
A	PHE216
A	ASN221
A	PHE244
A	PHE248
A	ASP252
A	HEM1002

site_id	AC5
Number of Residues	6
Details	binding site for residue LOP A 1006

Chain	Residue
A	ILE106
A	PHE113
A	TYR117
A	TYR118
A	ARG358
A	PHE367

site_id	AC6
Number of Residues	15
Details	binding site for residue HEC B 1001

Chain	Residue
B	VAL35
B	CYS36
B	CYS39
B	HIS40
B	ASN96
B	PRO98
B	MET103
B	ARG107
B	TYR130
B	LEU135
B	PHE160
B	ILE183
B	ALA184
B	MET185
B	PRO188

site_id	AC7
Number of Residues	4
Details	binding site for residue SR B 1002

Chain	Residue
B	ASP8
B	VAL9
B	GLU14
B	GLU129

site_id	AC8
Number of Residues	7
Details	binding site for residue FES C 1001

Chain	Residue
C	CYS129
C	HIS131
C	LEU132
C	CYS149
C	CYS151
C	HIS152
C	SER154

site_id	AC9
Number of Residues	17
Details	binding site for residue HEM E 1001

Chain	Residue
E	PHE104
E	THR142
E	GLY146
E	TYR147
E	LEU149
E	PRO150
E	HIS198
E	TYR199
E	PRO202
E	TYR297
E	GLN58
E	GLY62
E	ILE63
E	LEU65
E	ARG94
E	HIS97
E	ALA101

site_id	AD1
Number of Residues	18
Details	binding site for residue HEM E 1002

Chain	Residue
E	TRP45
E	GLY48
E	LEU51
E	PHE104
E	HIS111
E	ILE112
E	ARG114
E	SER120
E	ARG125
E	GLY132
E	MET133
E	ILE135
E	HIS212
E	PHE216
E	GLY220
E	ASN221
E	ASN222
E	ANJ1004

site_id	AD2
Number of Residues	14
Details	binding site for residue SMA E 1003

Chain	Residue
C	CYS151
C	HIS152
E	MET140
E	PHE144
E	MET154
E	GLY158
E	VAL161
E	ILE162
E	PRO294
E	GLU295
E	PHE298
E	TYR302
E	MET336
E	PHE337

site_id	AD3
Number of Residues	11
Details	binding site for residue ANJ E 1004

Chain	Residue
E	LEU41
E	TRP45
E	VAL49
E	ALA52
E	VAL209
E	ILE213
E	ASN221
E	PHE244
E	PHE248
E	ASP252
E	HEM1002

site_id	AD4
Number of Residues	7
Details	binding site for residue LOP E 1005

Chain	Residue
E	MET44
E	PHE113
E	TYR117
E	TYR118
E	VAL262
E	ARG358
E	TRP368

site_id	AD5
Number of Residues	4
Details	binding site for residue SR F 1002

Chain	Residue
F	ASP8
F	VAL9
F	GLU14
F	GLU129

site_id	AD6
Number of Residues	7
Details	binding site for residue FES G 1001

Chain	Residue
G	CYS129
G	HIS131
G	LEU132
G	CYS149
G	CYS151
G	HIS152
G	SER154

site_id	AD7
Number of Residues	15
Details	binding site for residue HEM K 1001

Chain	Residue
K	LEU55
K	GLN58
K	GLY62
K	LEU65
K	ALA66
K	ARG94
K	HIS97
K	THR142
K	GLY146
K	TYR147
K	LEU149
K	PRO150
K	HIS198
K	TYR199
K	PRO202

site_id	AD8
Number of Residues	19
Details	binding site for residue HEM K 1002

Chain	Residue
K	TRP45
K	GLY48
K	LEU51
K	ALA52
K	PHE104
K	HIS111
K	ARG114
K	SER120
K	ARG125
K	THR128
K	GLY132
K	MET133
K	ILE135
K	HIS212
K	PHE216
K	GLY220
K	ASN221
K	ASN222
K	ANJ1004

site_id	AD9
Number of Residues	16
Details	binding site for residue SMA K 1003

Chain	Residue
K	PHE144
K	MET145
K	MET154
K	GLY158
K	VAL161
K	ILE162
K	PHE194
K	LEU197
K	PRO294
K	GLU295
K	PHE298
K	TYR302
K	MET336
K	PHE337
Q	CYS151
Q	HIS152

site_id	AE1
Number of Residues	12
Details	binding site for residue ANJ K 1004

Chain	Residue
K	LEU41
K	TRP45
K	VAL49
K	ALA52
K	VAL209
K	ILE213
K	PHE216
K	ASN221
K	PHE244
K	PHE248
K	ASP252
K	HEM1002

site_id	AE2
Number of Residues	2
Details	binding site for residue SR K 1005

Chain	Residue
E	ASP311
K	ASP311

site_id	AE3
Number of Residues	9
Details	binding site for residue LOP K 1006

Chain	Residue
K	ASN42
K	TYR109
K	LEU110
K	PHE113
K	TYR117
K	TYR118
K	ARG358
K	PHE367
K	TRP368

site_id	AE4
Number of Residues	4
Details	binding site for residue SR L 1002

Chain	Residue
L	ASP8
L	VAL9
L	GLU14
L	GLU129

site_id	AE5
Number of Residues	7
Details	binding site for residue FES M 1001

Chain	Residue
M	CYS129
M	HIS131
M	LEU132
M	CYS149
M	CYS151
M	HIS152
M	SER154

site_id	AE6
Number of Residues	17
Details	binding site for residue HEM O 1001

Chain	Residue
O	LEU55
O	GLN58
O	GLY62
O	ILE63
O	LEU65
O	ARG94
O	HIS97
O	ALA101
O	THR142
O	GLY146
O	TYR147
O	LEU149
O	PRO150
O	HIS198
O	TYR199
O	PRO202
O	TYR297

site_id	AE7
Number of Residues	17
Details	binding site for residue HEM O 1002

Chain	Residue
O	TRP45
O	GLY48
O	LEU51
O	PHE104
O	HIS111
O	ARG114
O	SER120
O	ARG125
O	GLY132
O	MET133
O	ILE135
O	HIS212
O	PHE216
O	GLY220
O	ASN221
O	ASN222
O	ANJ1004

site_id	AE8
Number of Residues	13
Details	binding site for residue SMA O 1003

Chain	Residue
M	CYS151
M	HIS152
O	PHE144
O	MET154
O	GLY158
O	VAL161
O	ILE162
O	LEU197
O	PRO294
O	GLU295
O	PHE298
O	TYR302
O	MET336

site_id	AE9
Number of Residues	12
Details	binding site for residue ANJ O 1004

Chain	Residue
O	LEU41
O	TRP45
O	VAL49
O	ALA52
O	ILE213
O	PHE216
O	ASN221
O	PHE244
O	PHE248
O	LYS251
O	ASP252
O	HEM1002

site_id	AF1
Number of Residues	5
Details	binding site for residue LOP O 1005

Chain	Residue
O	LEU110
O	TYR117
O	TYR118
O	VAL262
O	ARG358

site_id	AF2
Number of Residues	4
Details	binding site for residue SR P 1002

Chain	Residue
P	ASP8
P	VAL9
P	GLU14
P	GLU129

site_id	AF3
Number of Residues	7
Details	binding site for residue FES Q 1001

Chain	Residue
Q	CYS129
Q	HIS131
Q	LEU132
Q	CYS149
Q	CYS151
Q	HIS152
Q	SER154

site_id	AF4
Number of Residues	18
Details	binding site for Di-peptide HEC F 1001 and CYS F 36

Chain	Residue
F	VAL31
F	TYR32
F	VAL35
F	ALA37
F	ALA38
F	CYS39
F	HIS40
F	ASN96
F	PRO98
F	MET103
F	ARG107
F	TYR130
F	LEU135
F	PHE160
F	ILE183
F	ALA184
F	MET185
F	PRO188

site_id	AF5
Number of Residues	20
Details	binding site for Di-peptide HEC F 1001 and CYS F 39

Chain	Residue
F	VAL35
F	CYS36
F	ALA37
F	ALA38
F	HIS40
F	SER92
F	ALA93
F	LEU94
F	ASN96
F	ALA97
F	PRO98
F	MET103
F	ARG107
F	TYR130
F	LEU135
F	PHE160
F	ILE183
F	ALA184
F	MET185
F	PRO188

site_id	AF6
Number of Residues	20
Details	binding site for Di-peptide HEC L 1001 and CYS L 39

Chain	Residue
A	SER233
L	VAL35
L	CYS36
L	ALA37
L	ALA38
L	HIS40
L	SER92
L	ALA93
L	LEU94
L	ASN96
L	ALA97
L	PRO98
L	MET103
L	ARG107
L	TYR130
L	LEU135
L	PHE160
L	ILE183
L	ALA184
L	MET185

site_id	AF7
Number of Residues	19
Details	binding site for Di-peptide HEC L 1001 and CYS L 36

Chain	Residue
A	SER233
L	VAL31
L	TYR32
L	VAL35
L	ALA37
L	ALA38
L	CYS39
L	HIS40
L	LEU94
L	ASN96
L	PRO98
L	MET103
L	ARG107
L	TYR130
L	LEU135
L	PHE160
L	ILE183
L	ALA184
L	MET185

site_id	AF8
Number of Residues	19
Details	binding site for Di-peptide HEC P 1001 and CYS P 39

Chain	Residue
P	VAL35
P	CYS36
P	ALA37
P	ALA38
P	HIS40
P	SER92
P	ALA93
P	LEU94
P	ASN96
P	ALA97
P	PRO98
P	MET103
P	ARG107
P	TYR130
P	LEU135
P	PHE160
P	ILE183
P	ALA184
P	MET185

site_id	AF9
Number of Residues	17
Details	binding site for Di-peptide HEC P 1001 and CYS P 36

Chain	Residue
P	VAL31
P	TYR32
P	VAL35
P	ALA37
P	ALA38
P	CYS39
P	HIS40
P	ASN96
P	PRO98
P	MET103
P	ARG107
P	TYR130
P	LEU135
P	PHE160
P	ILE183
P	ALA184
P	MET185

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	580
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	528
Details	Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	268
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	20
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	72
Details	Transmembrane: {"description":"Helical; Note=Anchors to the membrane","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"description":"covalent"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	80
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	384
Details	Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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