Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2YBB

Fitted model for bovine mitochondrial supercomplex I1III2IV1 by single particle cryo-EM (EMD-1876)

Functional Information from GO Data

Chain	GOid	namespace	contents
1	0005886	cellular_component	plasma membrane
1	0008137	molecular_function	NADH dehydrogenase (ubiquinone) activity
1	0010181	molecular_function	FMN binding
1	0046872	molecular_function	metal ion binding
1	0048038	molecular_function	quinone binding
1	0051287	molecular_function	NAD binding
1	0051536	molecular_function	iron-sulfur cluster binding
1	0051539	molecular_function	4 iron, 4 sulfur cluster binding
1	1902600	biological_process	proton transmembrane transport
2	0003954	molecular_function	NADH dehydrogenase activity
2	0005886	cellular_component	plasma membrane
2	0016491	molecular_function	oxidoreductase activity
2	0046872	molecular_function	metal ion binding
2	0048038	molecular_function	quinone binding
2	0051536	molecular_function	iron-sulfur cluster binding
2	0051537	molecular_function	2 iron, 2 sulfur cluster binding
3	0005886	cellular_component	plasma membrane
3	0008137	molecular_function	NADH dehydrogenase (ubiquinone) activity
3	0016020	cellular_component	membrane
3	0016491	molecular_function	oxidoreductase activity
3	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
3	0042773	biological_process	ATP synthesis coupled electron transport
3	0043546	molecular_function	molybdopterin cofactor binding
3	0046872	molecular_function	metal ion binding
3	0048038	molecular_function	quinone binding
3	0051536	molecular_function	iron-sulfur cluster binding
3	0051537	molecular_function	2 iron, 2 sulfur cluster binding
3	0051539	molecular_function	4 iron, 4 sulfur cluster binding
3	1902600	biological_process	proton transmembrane transport
4	0005886	cellular_component	plasma membrane
4	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
4	0048038	molecular_function	quinone binding
4	0050136	molecular_function	NADH dehydrogenase (quinone) (non-electrogenic) activity
4	0051287	molecular_function	NAD binding
5	0005886	cellular_component	plasma membrane
5	0008137	molecular_function	NADH dehydrogenase (ubiquinone) activity
5	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
5	0048038	molecular_function	quinone binding
5	0050136	molecular_function	NADH dehydrogenase (quinone) (non-electrogenic) activity
5	1902600	biological_process	proton transmembrane transport
6	0005506	molecular_function	iron ion binding
6	0005886	cellular_component	plasma membrane
6	0008137	molecular_function	NADH dehydrogenase (ubiquinone) activity
6	0009060	biological_process	aerobic respiration
6	0015990	biological_process	electron transport coupled proton transport
6	0045271	cellular_component	respiratory chain complex I
6	0046872	molecular_function	metal ion binding
6	0048038	molecular_function	quinone binding
6	0050136	molecular_function	NADH dehydrogenase (quinone) (non-electrogenic) activity
6	0051536	molecular_function	iron-sulfur cluster binding
6	0051539	molecular_function	4 iron, 4 sulfur cluster binding
7	0005886	cellular_component	plasma membrane
7	0008199	molecular_function	ferric iron binding
7	0016226	biological_process	iron-sulfur cluster assembly
7	0048038	molecular_function	quinone binding
8	0003954	molecular_function	NADH dehydrogenase activity
8	0005506	molecular_function	iron ion binding
8	0005886	cellular_component	plasma membrane
8	0009060	biological_process	aerobic respiration
8	0016020	cellular_component	membrane
8	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
8	0046872	molecular_function	metal ion binding
8	0048038	molecular_function	quinone binding
8	0050136	molecular_function	NADH dehydrogenase (quinone) (non-electrogenic) activity
8	0051536	molecular_function	iron-sulfur cluster binding
8	0051539	molecular_function	4 iron, 4 sulfur cluster binding
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	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	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	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
I	0008121	molecular_function	quinol-cytochrome-c reductase activity
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
K	0005739	cellular_component	mitochondrion
K	0005743	cellular_component	mitochondrial inner membrane
K	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
K	0022904	biological_process	respiratory electron transport chain
K	0045275	cellular_component	respiratory chain complex III
L	0004129	molecular_function	cytochrome-c oxidase activity
L	0005743	cellular_component	mitochondrial inner membrane
L	0006119	biological_process	oxidative phosphorylation
L	0009060	biological_process	aerobic respiration
L	0016020	cellular_component	membrane
L	0020037	molecular_function	heme binding
L	0022904	biological_process	respiratory electron transport chain
L	0045277	cellular_component	respiratory chain complex IV
L	0046872	molecular_function	metal ion binding
L	1902600	biological_process	proton transmembrane transport
M	0004129	molecular_function	cytochrome-c oxidase activity
M	0005507	molecular_function	copper ion binding
M	0005739	cellular_component	mitochondrion
M	0005743	cellular_component	mitochondrial inner membrane
M	0016020	cellular_component	membrane
M	0016491	molecular_function	oxidoreductase activity
M	0017004	biological_process	cytochrome complex assembly
M	0022900	biological_process	electron transport chain
M	0022904	biological_process	respiratory electron transport chain
M	0031966	cellular_component	mitochondrial membrane
M	0042773	biological_process	ATP synthesis coupled electron transport
M	0045277	cellular_component	respiratory chain complex IV
M	0046872	molecular_function	metal ion binding
M	1902600	biological_process	proton transmembrane transport
N	0004129	molecular_function	cytochrome-c oxidase activity
N	0005739	cellular_component	mitochondrion
N	0005743	cellular_component	mitochondrial inner membrane
N	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
N	0008535	biological_process	respiratory chain complex IV assembly
N	0009055	molecular_function	electron transfer activity
N	0016020	cellular_component	membrane
N	0019646	biological_process	aerobic electron transport chain
N	0022904	biological_process	respiratory electron transport chain
N	0045277	cellular_component	respiratory chain complex IV
N	1902600	biological_process	proton transmembrane transport
O	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
O	0045277	cellular_component	respiratory chain complex IV
P	0005743	cellular_component	mitochondrial inner membrane
P	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
P	0045277	cellular_component	respiratory chain complex IV
Q	0005740	cellular_component	mitochondrial envelope
Q	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
Q	0045277	cellular_component	respiratory chain complex IV
R	0005743	cellular_component	mitochondrial inner membrane
S	0005739	cellular_component	mitochondrion
S	0005743	cellular_component	mitochondrial inner membrane
S	0006119	biological_process	oxidative phosphorylation
S	0016020	cellular_component	membrane
S	0045277	cellular_component	respiratory chain complex IV
T	0005743	cellular_component	mitochondrial inner membrane
T	0006119	biological_process	oxidative phosphorylation
T	0016020	cellular_component	membrane
T	0045277	cellular_component	respiratory chain complex IV
U	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
U	0045277	cellular_component	respiratory chain complex IV
V	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
W	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
W	0045277	cellular_component	respiratory chain complex IV
X	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
X	0045277	cellular_component	respiratory chain complex IV
Y	0005758	cellular_component	mitochondrial intermembrane space
Y	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
Y	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
Y	0006915	biological_process	apoptotic process
Y	0009055	molecular_function	electron transfer activity
Y	0020037	molecular_function	heme binding
Y	0022904	biological_process	respiratory electron transport chain
Y	0046872	molecular_function	metal ion binding
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	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	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	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
i	0008121	molecular_function	quinol-cytochrome-c reductase activity
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
k	0005739	cellular_component	mitochondrion
k	0005743	cellular_component	mitochondrial inner membrane
k	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
k	0022904	biological_process	respiratory electron transport chain
k	0045275	cellular_component	respiratory chain complex III

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 1 439

Chain	Residue
1	PRO199
1	SER352
1	CYS353
1	LYS355
1	CYS356
1	CYS359
1	SER398
1	PHE399
1	CYS400

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE FMN 1 440

Chain	Residue
1	GLY64
1	ARG65
1	GLY66
1	LYS75
1	ASN92
1	ASP94
1	SER96
1	GLY183
1	GLU184
1	GLU185
1	ILE218
1	ASN219
1	ASN220
1	THR223
1	PRO401
1	NAI441

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NAI 1 441

Chain	Residue
1	GLY66
1	GLY67
1	ALA68
1	PHE70
1	LYS75
1	PHE78
1	GLU97
1	TYR180
1	GLU185
1	LYS202
1	PHE205
1	THR325
1	PRO401
1	FMN440

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG 1 442

Chain	Residue
1	HIS35

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES 2 182

Chain	Residue
2	CYS83
2	SER87
2	CYS88
2	CYS124
2	LEU125
2	GLY126
2	SER127
2	CYS128

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG 2 206

Chain	Residue
1	HIS350
2	SER68
2	GLU123

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 3 784

Chain	Residue
3	HIS115
3	CYS119
3	CYS122
3	CYS128
3	LEU130
3	VAL232
3	GLY233

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 3 785

Chain	Residue
3	CYS181
3	ILE182
3	CYS184
3	ARG186
3	CYS187
3	CYS230
3	VAL232
3	ALA234

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 3 786

Chain	Residue
3	CYS256
3	CYS259
3	VAL261
3	GLY262
3	CYS263
3	ILE290
3	CYS291
3	PRO407
3	ILE408

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES 3 787

Chain	Residue
3	CYS34
3	SER35
3	GLY43
3	ALA44
3	CYS45
3	ARG46
3	CYS48
3	CYS83

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG 3 788

Chain	Residue
3	LEU274
3	ASP302

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG 3 789

Chain	Residue
3	HIS167
7	GLU32

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG 4 410

Chain	Residue
4	VAL223
4	ALA384
4	LYS386
4	GLU388

site_id	BC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG 5 208

Chain	Residue
5	HIS144

site_id	BC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 6 182

Chain	Residue
6	CYS111
6	CYS140
6	PRO141
4	ARG84
4	HIS169
6	CYS45
6	CYS46
6	GLY82
6	ARG83
6	ALA110

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA 7 204

Chain	Residue
3	ASP165
3	HIS168
7	GLU32
7	GLU34
7	SER60
7	GLY64

site_id	BC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 8 183

Chain	Residue
8	HIS41
8	CYS63
8	ILE68
8	CYS98
8	ILE99
8	PHE100
8	CYS101
8	GLY102
8	CYS104

site_id	BC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 8 184

Chain	Residue
8	CYS53
8	ILE54
8	CYS56
8	SER57
8	CYS59
8	CYS108
8	THR110
8	ALA112

site_id	CC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM C 501

Chain	Residue
C	GLN44
C	GLY48
C	LEU49
C	LEU51
C	ARG80
C	HIS83
C	PHE90
C	ALA127
C	GLY130
C	TYR131
C	HIS182
C	PHE183
C	PRO186
C	HOH2077
C	HOH2102

site_id	CC2
Number of Residues	16
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	LEU197
C	LEU200
C	SER205
C	ASN206
C	UQ12002
C	HOH2015
C	HOH2038

site_id	CC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SMA C 2001

Chain	Residue
C	LEU121
C	MET129
C	MET138
C	GLY142
C	VAL145
C	ILE146
C	PRO270
C	GLU271
C	PHE274
C	TYR278
C	HOH2052
e	CYS160
e	HIS161

site_id	CC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE UQ1 C 2002

Chain	Residue
C	LEU21
C	SER35
C	LEU197
C	HIS201
C	SER205
C	PHE220
C	ASP228
C	HEM502
C	HOH2044

site_id	CC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEC D 501

Chain	Residue
D	VAL36
D	CYS37
D	CYS40
D	HIS41
D	ASN105
D	LEU109
D	PRO110
D	PRO111
D	ILE116
D	ARG120
D	TYR126
D	PHE153
D	ILE158
D	GLY159
D	MET160
D	PRO163
D	ILE164
D	HOH4040
D	HOH4053
D	HOH4094
D	HOH4113

site_id	CC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES E 501

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

site_id	CC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CDL G 2003

Chain	Residue
C	SER29
C	LEU36
C	LYS227
C	LEU234
C	LEU235
D	TYR220
D	LYS223
D	ARG224
D	LYS231
F	MET70
F	ARG71
G	TYR29
G	ILE34
G	ASN36
G	ARG40
G	HOH1515
G	CDL2004

site_id	CC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CDL G 2004

Chain	Residue
C	SER28
C	SER29
C	TRP30
C	PHE33
C	HOH2094
F	GLN72
G	ARG40
G	THR41
G	HOH1045
G	HOH1254
G	CDL2003

site_id	CC9
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEA L 515

Chain	Residue
L	GLY27
L	MET28
L	SER34
L	ILE37
L	ARG38
L	TYR54
L	VAL58
L	HIS61
L	ALA62
L	MET65
L	ILE66
L	VAL70
L	GLY125
L	TRP126
L	TYR371
L	PHE377
L	HIS378
L	SER382
L	PHE425
L	GLN428
L	ARG438
L	ARG439
L	MET468

site_id	DC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEA L 516

Chain	Residue
L	TRP126
L	TRP236
L	VAL243
L	TYR244
L	HIS290
L	HIS291
L	THR309
L	ALA313
L	THR316
L	GLY317
L	GLY352
L	LEU353
L	GLY355
L	ILE356
L	LEU358
L	ALA359
L	ASP364
L	HIS368
L	HIS376
L	PHE377
L	VAL380
L	ARG438

site_id	DC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU L 517

Chain	Residue
L	HIS240
L	HIS290
L	HIS291

site_id	DC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG L 518

Chain	Residue
L	HIS368
L	ASP369
M	GLU198

site_id	DC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU M 228

Chain	Residue
M	HIS161
M	CYS196
M	CYS200
M	MET207
M	CU229

site_id	DC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU M 229

Chain	Residue
M	CYS196
M	GLU198
M	CYS200
M	HIS204
M	CU228

site_id	DC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN Q 99

Chain	Residue
Q	CYS60
Q	CYS62
Q	CYS82
Q	CYS85

site_id	DC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM Y 500

Chain	Residue
Y	LYS13
Y	CYS14
Y	GLN16
Y	CYS17
Y	HIS18
Y	THR28
Y	PRO30
Y	THR40
Y	GLY41
Y	TYR48
Y	THR49
Y	ASN52
Y	TRP59
Y	TYR67
Y	LEU68
Y	THR78
Y	LYS79
Y	MET80
Y	ILE81
Y	PHE82
Y	HOH205
Y	HOH217
Y	HOH225

site_id	DC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM c 501

Chain	Residue
c	GLN44
c	GLY48
c	LEU49
c	LEU51
c	ARG80
c	HIS83
c	PHE90
c	ALA127
c	GLY130
c	TYR131
c	HIS182
c	PHE183
c	PRO186
c	HOH3067
c	HOH3108

site_id	DC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM c 502

Chain	Residue
c	TRP31
c	GLY34
c	LEU37
c	HIS97
c	VAL98
c	ARG100
c	SER106
c	THR112
c	GLY116
c	VAL117
c	HIS196
c	LEU200
c	SER205
c	ASN206
c	UQ13002
c	HOH3015
c	HOH3033

site_id	EC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SMA c 3001

Chain	Residue
E	CYS160
E	HIS161
c	LEU121
c	MET129
c	MET138
c	GLY142
c	VAL145
c	ILE146
c	PRO270
c	GLU271
c	PHE274
c	TYR278
c	HOH3090

site_id	EC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE UQ1 c 3002

Chain	Residue
c	LEU21
c	SER35
c	HIS201
c	SER205
c	PHE220
c	ASP228
c	HEM502
c	HOH3110
c	HOH3116

site_id	EC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEC d 501

Chain	Residue
Y	HOH308
d	VAL36
d	CYS37
d	CYS40
d	HIS41
d	ASN105
d	LEU109
d	PRO110
d	PRO111
d	ARG120
d	TYR126
d	PHE153
d	ILE158
d	GLY159
d	MET160
d	PRO163
d	ILE164
d	HOH3035
d	HOH3047

site_id	EC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CDL d 3003

Chain	Residue
c	SER29
c	ASN32
c	LEU36
c	LYS227
c	LEU234
c	ALA238
d	TYR220
d	LYS223
d	ARG224
d	LYS231
d	HOH3091
f	MET70
f	ARG71
f	GLN72
g	TYR29
g	ILE34
g	ASN36
g	ARG40
g	CDL3004

site_id	EC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES e 501

Chain	Residue
e	CYS139
e	HIS141
e	LEU142
e	CYS144
e	CYS158
e	HIS161
e	SER163

site_id	EC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CDL g 3004

Chain	Residue
c	SER28
c	SER29
c	TRP30
d	CDL3003
f	GLN72
g	ARG40
g	THR41
g	HOH3016
g	HOH3017
g	HOH3026

Functional Information from PROSITE/UniProt

site_id	PS00077
Number of Residues	56
Details	COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyililpgfgmishivtyysgkkepfgymgmvwammsigflgfivwa.HH

Chain	Residue	Details
L	TRP236-HIS291

site_id	PS00078
Number of Residues	49
Details	COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VlHswavpslglktdaipgrlnqttlmssrpglyygq......CseiCgsnHsfM

Chain	Residue	Details
M	VAL159-MET207

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

Chain	Residue	Details
b	GLY54-THR77

site_id	PS00198
Number of Residues	12
Details	4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiGCSlCAaACP

Chain	Residue	Details
8	CYS53-PRO64
8	CYS98-PRO109

site_id	PS00535
Number of Residues	12
Details	COMPLEX1_49K Respiratory chain NADH dehydrogenase 49 Kd subunit signature. LHTGfEKTmEhR

Chain	Residue	Details
4	LEU62-ARG73

site_id	PS00542
Number of Residues	22
Details	COMPLEX1_30K Respiratory chain NADH dehydrogenase 30 Kd subunit signature. EREvyDLFgivfegHpdlRkIL

Chain	Residue	Details
5	GLU115-LEU136

site_id	PS00641
Number of Residues	18
Details	COMPLEX1_75K_1 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. PlfCSekhlspiGaCRmC

Chain	Residue	Details
3	PRO31-CYS48

site_id	PS00642
Number of Residues	13
Details	COMPLEX1_75K_2 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. CPtCDkGGaCeLQ

Chain	Residue	Details
3	CYS119-GLN131

site_id	PS00643
Number of Residues	11
Details	COMPLEX1_75K_3 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. RCIhCkRCVrY

Chain	Residue	Details
3	ARG180-TYR190

site_id	PS00644
Number of Residues	16
Details	COMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GAGAYICGEETALMNS

Chain	Residue	Details
1	GLY176-SER191

site_id	PS00645
Number of Residues	12
Details	COMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ESCGkCtPCReG

Chain	Residue	Details
1	GLU351-GLY362

site_id	PS00848
Number of Residues	23
Details	COX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. VIWfwlhkgeaqrCpsCGthYKL

Chain	Residue	Details
Q	VAL69-LEU91

site_id	PS01099
Number of Residues	19
Details	COMPLEX1_24K Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. DglFSvqkveCLGsChtAP

Chain	Residue	Details
2	ASP114-PRO132

site_id	PS01150
Number of Residues	17
Details	COMPLEX1_20K Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. NvDSVVPVDVYvPgCPP

Chain	Residue	Details
6	ASN126-PRO142

site_id	PS01329
Number of Residues	18
Details	COX6A Cytochrome c oxidase subunit VIa signature. IRtKpFsWGDGnHTfFhN

Chain	Residue	Details
R	ILE55-ASN72

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	47
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16469879","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	39
Details	Domain: {"description":"4Fe-4S His(Cys)3-ligated-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	56
Details	Domain: {"description":"4Fe-4S Mo/W bis-MGD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01004","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16469879","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	30
Details	Domain: {"description":"4Fe-4S ferredoxin-type 1"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	29
Details	Domain: {"description":"4Fe-4S ferredoxin-type 2"}

Chain

Residue

Details

site_id	SWS_FT_FI9
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_FI10
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_FI11
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_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q68FY0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
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_FI14
Number of Residues	322
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"1L0L","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
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_FI16
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_FI17
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_FI18
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_FI19
Number of Residues	658
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	244
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	178
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
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_FI23
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_FI24
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_FI25
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_FI26
Number of Residues	170
Details	Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	10
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_FI28
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_FI29
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_FI30
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_FI31
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P99028","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	75
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	76
Details	Transmembrane: {"description":"Helical; Name=I","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	9
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	87
Details	Transmembrane: {"description":"Helical; Name=II","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	54
Details	Transmembrane: {"description":"Helical; Name=III","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	47
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	52
Details	Transmembrane: {"description":"Helical; Name=IV","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	56
Details	Transmembrane: {"description":"Helical; Name=V","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	65
Details	Transmembrane: {"description":"Helical; Name=VI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	39
Details	Transmembrane: {"description":"Helical; Name=VII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	28
Details	Transmembrane: {"description":"Helical; Name=VIII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI43
Number of Residues	120
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI44
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=IX","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI45
Number of Residues	279
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI46
Number of Residues	29
Details	Transmembrane: {"description":"Helical; Name=X","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI47
Number of Residues	26
Details	Transmembrane: {"description":"Helical; Name=XI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI48
Number of Residues	31
Details	Transmembrane: {"description":"Helical; Name=XII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI49
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23537388","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI50
Number of Residues	3
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI51
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI52
Number of Residues	1
Details	Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI53
Number of Residues	2
Details	Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"PubMed","id":"10338009","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI54
Number of Residues	1
Details	Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"220175","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI55
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00406","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI56
Number of Residues	192
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI57
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI58
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P13073","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI59
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10888","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI60
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI61
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P12787","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI62
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P20674","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI63
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI64
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19536","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI65
Number of Residues	46
Details	Domain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI66
Number of Residues	10
Details	Motif: {"description":"Cx9C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI67
Number of Residues	11
Details	Motif: {"description":"Cx10C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI68
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56391","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI69
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17665","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI70
Number of Residues	2
Details	Binding site: {"description":"covalent"}

Chain

Residue

Details

site_id	SWS_FT_FI71
Number of Residues	2
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

site_id	SWS_FT_FI72
Number of Residues	1
Details	Modified residue: {"description":"N-acetylglycine","evidences":[{"source":"PubMed","id":"5933874","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI73
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"16866357","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI74
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI75
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI76
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18471988","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI77
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	14
Details	M-CSA 124

Chain	Residue	Details
T	GLU61	metal ligand

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)