Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3H1J

Stigmatellin-bound cytochrome bc1 complex from chicken

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0046872	molecular_function	metal ion binding
B	0005743	cellular_component	mitochondrial inner membrane
B	0045275	cellular_component	respiratory chain complex III
B	0046872	molecular_function	metal ion binding
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
C	0006979	biological_process	response to oxidative stress
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	0045275	cellular_component	respiratory chain complex III
C	1902600	biological_process	proton transmembrane transport
D	0005743	cellular_component	mitochondrial inner membrane
D	0009055	molecular_function	electron transfer activity
D	0020037	molecular_function	heme binding
D	0045275	cellular_component	respiratory chain complex III
E	0008121	molecular_function	quinol-cytochrome-c reductase activity
E	0016020	cellular_component	membrane
E	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0005743	cellular_component	mitochondrial inner membrane
F	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
F	0045275	cellular_component	respiratory chain complex III
G	0005743	cellular_component	mitochondrial inner membrane
G	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
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	0045275	cellular_component	respiratory chain complex III
I	0008121	molecular_function	quinol-cytochrome-c reductase activity
J	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
J	0045275	cellular_component	respiratory chain complex III
N	0046872	molecular_function	metal ion binding
O	0005743	cellular_component	mitochondrial inner membrane
O	0045275	cellular_component	respiratory chain complex III
O	0046872	molecular_function	metal ion binding
P	0005737	cellular_component	cytoplasm
P	0005739	cellular_component	mitochondrion
P	0005743	cellular_component	mitochondrial inner membrane
P	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
P	0006979	biological_process	response to oxidative stress
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	0045275	cellular_component	respiratory chain complex III
P	1902600	biological_process	proton transmembrane transport
Q	0005743	cellular_component	mitochondrial inner membrane
Q	0009055	molecular_function	electron transfer activity
Q	0020037	molecular_function	heme binding
Q	0045275	cellular_component	respiratory chain complex III
R	0008121	molecular_function	quinol-cytochrome-c reductase activity
R	0016020	cellular_component	membrane
R	0051537	molecular_function	2 iron, 2 sulfur cluster binding
S	0005743	cellular_component	mitochondrial inner membrane
S	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
S	0045275	cellular_component	respiratory chain complex III
T	0005743	cellular_component	mitochondrial inner membrane
T	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
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	0045275	cellular_component	respiratory chain complex III
V	0008121	molecular_function	quinol-cytochrome-c reductase activity
W	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
W	0045275	cellular_component	respiratory chain complex III

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM C 501

Chain	Residue
C	GLN45
C	THR127
C	GLY131
C	TYR132
C	LEU134
C	PRO135
C	HIS183
C	PHE184
C	PRO187
C	ILE190
C	GLY49
C	LEU50
C	LEU52
C	ALA53
C	ARG81
C	HIS84
C	ALA88
C	LEU124

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM C 502

Chain	Residue
C	TRP32
C	GLY35
C	LEU38
C	ALA39
C	HIS98
C	ARG101
C	SER107
C	TRP114
C	GLY117
C	VAL118
C	LEU120
C	HIS197
C	LEU198
C	SER206
C	ASN207
C	HOH381
C	HOH384
C	UQ2002

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SMA C 2001

Chain	Residue
C	MET125
C	GLY143
C	VAL146
C	ILE147
C	LEU182
C	LYS270
C	PRO271
C	GLU272
C	PHE275
C	TYR279
C	LEU295
R	CYS160
R	HIS161

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE UQ C 2002

Chain	Residue
C	LEU22
C	ILE28
C	ALA39
C	LEU198
C	HIS202
C	SER206
C	PHE221
C	ASP229
C	HOH385
C	HEM502

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PEE C 2007

Chain	Residue
C	TRP31
C	PHE96
C	TYR104
C	TYR105
C	PHE277
C	THR317
C	TRP327
F	TYR29
G	GLN44
G	CDL2004

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEE C 2008

Chain	Residue
A	SER439
A	TYR442
C	HIS222
E	PEE2005

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE UNL C 2010

Chain	Residue
C	TYR274

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 2011

Chain	Residue
C	PHE64
C	ARG81
C	ASN256
D	TYR115

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE UNL C 2104

Chain	Residue
C	HIS159

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE UNL C 3015

Chain	Residue
C	THR199
C	HIS202

site_id	BC2
Number of Residues	15
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	ILE116
D	ARG120
D	TYR126
D	PHE153
D	ILE158
D	GLY159
D	MET160
D	PRO163

site_id	BC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CDL D 2003

Chain	Residue
C	MET236
D	TYR220
D	LYS223
D	ARG224
D	LYS231
F	HIS72
F	ARG73
G	ILE29
G	ARG40
G	CDL2004
C	ALA30
C	LYS228
C	GLY232

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES E 501

Chain	Residue
E	CYS139
E	HIS141
E	LEU142
E	CYS144
E	CYS158
E	CYS160
E	HIS161
E	SER163

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PEE E 2005

Chain	Residue
A	TYR442
C	PHE227
C	PEE2008
E	TYR37
E	THR40
E	THR47
J	PHE14
J	PHE20
J	VAL25
J	GLU32

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PLC E 2009

Chain	Residue
C	LEU79
D	GLN200
D	MET204
D	LYS207
E	TYR49
E	ALA50
E	ASN53
E	GLN57
J	ASP36

site_id	BC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE UNL E 2105

Chain	Residue
E	TYR178

site_id	BC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE UNL E 3103

Chain	Residue
E	THR140
P	UNL3104

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CDL G 2004

Chain	Residue
C	SER29
C	ALA30
C	TRP31
C	TYR105
C	PEE2007
D	CDL2003
F	HIS72
G	ARG40
G	GLN44

site_id	CC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEE N 3008

Chain	Residue
N	TYR442
P	HIS222

site_id	CC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM P 501

Chain	Residue
P	GLN45
P	GLY49
P	LEU50
P	LEU52
P	ALA53
P	ARG81
P	HIS84
P	LEU124
P	THR127
P	GLY131
P	TYR132
P	LEU134
P	PRO135
P	HIS183
P	PHE184
P	PRO187
P	ILE190

site_id	CC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM P 502

Chain	Residue
P	TRP32
P	GLY35
P	LEU38
P	ALA39
P	HIS98
P	ARG101
P	SER107
P	TRP114
P	GLY117
P	VAL118
P	LEU120
P	HIS197
P	LEU198
P	SER206
P	ASN207
P	HOH381
P	HOH384

site_id	CC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE SMA P 3001

Chain	Residue
E	CYS160
E	HIS161
P	PHE129
P	GLY143
P	VAL146
P	PHE179
P	LYS270
P	PRO271
P	GLU272
P	PHE275
P	TYR279
P	LEU295

site_id	CC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE UQ P 3002

Chain	Residue
P	LEU22
P	ILE28
P	ALA39
P	LEU198
P	HIS202
P	SER206
P	PHE221
P	TYR225
P	ASP229
P	HOH382

site_id	CC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CDL P 3004

Chain	Residue
P	SER29
P	ALA30
P	TRP31
P	TYR105
P	PEE3007
S	HIS72
S	CDL3003
T	ARG40
T	PHE41
T	GLN44

site_id	CC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PEE P 3007

Chain	Residue
P	TRP31
P	TYR104
P	TYR105
P	PHE277
P	THR317
P	TRP327
P	CDL3004
S	TYR29
T	GLN44

site_id	CC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE UNL P 3010

Chain	Residue
P	TYR274

site_id	CC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL P 3011

Chain	Residue
P	PHE64
P	ARG81
P	ASN256
P	PHE257
Q	TYR115

site_id	DC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE UNL P 3104

Chain	Residue
E	UNL3103
P	ASN149

site_id	DC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEC Q 501

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

site_id	DC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES R 501

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

site_id	DC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE UNL R 2103

Chain	Residue
R	CYS139
R	GLY143

site_id	DC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PEE R 3005

Chain	Residue
N	TYR442
P	PHE227
R	TYR37
R	THR40
R	THR47
W	PHE14
W	ARG15
W	PHE20
W	ALA21
W	VAL25
W	GLU32

site_id	DC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PLC R 3009

Chain	Residue
P	LEU79
P	LEU241
Q	GLN200
Q	MET204
Q	LYS207
R	TYR49
R	ALA50
R	ASN53
R	GLN57
W	ASP36

site_id	DC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CDL S 3003

Chain	Residue
P	ALA30
P	ASN33
P	LYS228
P	GLY232
P	MET236
P	CDL3004
Q	TYR220
Q	LYS223
Q	ARG224
Q	LYS231
S	HIS72
S	ARG73
T	ILE29
T	ARG40

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI3
Number of Residues	322
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"20025846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21575592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22690928","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3L70","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00968","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20025846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21575592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22690928","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L70","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L71","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L72","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L73","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L74","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L75","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TGU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20025846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21575592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22690928","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CWB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L70","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L71","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L72","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L73","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L74","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L75","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TGU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20025846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21575592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22690928","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L70","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L71","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L72","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L73","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L74","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L75","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TGU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21575592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22690928","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CWB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L72","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	54
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"UniProtKB","id":"P13272","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	66
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	266
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"UniProtKB","id":"P13272","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	170
Details	Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3H1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3H1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1I","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1hr6

Chain	Residue	Details
A	GLU60

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1hr6

Chain	Residue	Details
N	GLU60

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1hr6

Chain	Residue	Details
B	ARG70

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1hr6

Chain	Residue	Details
O	ARG70

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