Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6YMX

CIII2/CIV respiratory supercomplex from Saccharomyces cerevisiae

Functional Information from GO Data

Chain	GOid	namespace	contents
a	0004129	molecular_function	cytochrome-c oxidase activity
a	0005515	molecular_function	protein binding
a	0005739	cellular_component	mitochondrion
a	0005743	cellular_component	mitochondrial inner membrane
a	0006119	biological_process	oxidative phosphorylation
a	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
a	0009060	biological_process	aerobic respiration
a	0016020	cellular_component	membrane
a	0020037	molecular_function	heme binding
a	0022904	biological_process	respiratory electron transport chain
a	0031966	cellular_component	mitochondrial membrane
a	0045277	cellular_component	respiratory chain complex IV
a	0045333	biological_process	cellular respiration
a	0046872	molecular_function	metal ion binding
a	1902600	biological_process	proton transmembrane transport
A	0004222	molecular_function	metalloendopeptidase activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
A	0006627	biological_process	protein processing involved in protein targeting to mitochondrion
A	0008121	molecular_function	quinol-cytochrome-c reductase activity
A	0009060	biological_process	aerobic respiration
A	0017087	cellular_component	mitochondrial processing peptidase complex
A	0022904	biological_process	respiratory electron transport chain
A	0045275	cellular_component	respiratory chain complex III
A	0045333	biological_process	cellular respiration
A	0046872	molecular_function	metal ion binding
A	1902600	biological_process	proton transmembrane transport
b	0004129	molecular_function	cytochrome-c oxidase activity
b	0005507	molecular_function	copper ion binding
b	0005515	molecular_function	protein binding
b	0005739	cellular_component	mitochondrion
b	0005743	cellular_component	mitochondrial inner membrane
b	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
b	0009060	biological_process	aerobic respiration
b	0016020	cellular_component	membrane
b	0016491	molecular_function	oxidoreductase activity
b	0022900	biological_process	electron transport chain
b	0022904	biological_process	respiratory electron transport chain
b	0031966	cellular_component	mitochondrial membrane
b	0042773	biological_process	ATP synthesis coupled electron transport
b	0045277	cellular_component	respiratory chain complex IV
b	0046872	molecular_function	metal ion binding
b	1902600	biological_process	proton transmembrane transport
B	0004222	molecular_function	metalloendopeptidase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
B	0006508	biological_process	proteolysis
B	0008121	molecular_function	quinol-cytochrome-c reductase activity
B	0009060	biological_process	aerobic respiration
B	0016020	cellular_component	membrane
B	0022904	biological_process	respiratory electron transport chain
B	0030061	cellular_component	mitochondrial crista
B	0045275	cellular_component	respiratory chain complex III
B	0045333	biological_process	cellular respiration
B	0046872	molecular_function	metal ion binding
B	1902600	biological_process	proton transmembrane transport
c	0004129	molecular_function	cytochrome-c oxidase activity
c	0005739	cellular_component	mitochondrion
c	0005743	cellular_component	mitochondrial inner membrane
c	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
c	0009055	molecular_function	electron transfer activity
c	0009060	biological_process	aerobic respiration
c	0016020	cellular_component	membrane
c	0019646	biological_process	aerobic electron transport chain
c	0022904	biological_process	respiratory electron transport chain
c	0031966	cellular_component	mitochondrial membrane
c	0045277	cellular_component	respiratory chain complex IV
c	0045333	biological_process	cellular respiration
c	0048039	molecular_function	ubiquinone binding
c	1902600	biological_process	proton transmembrane transport
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	0009060	biological_process	aerobic respiration
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0022904	biological_process	respiratory electron transport chain
C	0045275	cellular_component	respiratory chain complex III
C	0045333	biological_process	cellular respiration
C	0046872	molecular_function	metal ion binding
C	1902600	biological_process	proton transmembrane transport
d	0005740	cellular_component	mitochondrial envelope
d	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
d	0045277	cellular_component	respiratory chain complex IV
D	0009055	molecular_function	electron transfer activity
D	0020037	molecular_function	heme binding
e	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
e	0045277	cellular_component	respiratory chain complex IV
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	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
f	0045277	cellular_component	respiratory chain complex IV
F	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
g	0004129	molecular_function	cytochrome-c oxidase activity
g	0005739	cellular_component	mitochondrion
g	0005743	cellular_component	mitochondrial inner membrane
g	0006119	biological_process	oxidative phosphorylation
g	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
g	0016491	molecular_function	oxidoreductase activity
g	0031966	cellular_component	mitochondrial membrane
g	0045277	cellular_component	respiratory chain complex IV
g	0045333	biological_process	cellular respiration
g	1902600	biological_process	proton transmembrane transport
G	0005739	cellular_component	mitochondrion
G	0005743	cellular_component	mitochondrial inner membrane
G	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
G	0008121	molecular_function	quinol-cytochrome-c reductase activity
G	0009060	biological_process	aerobic respiration
G	0016020	cellular_component	membrane
G	0022904	biological_process	respiratory electron transport chain
G	0034551	biological_process	mitochondrial respiratory chain complex III assembly
G	0045275	cellular_component	respiratory chain complex III
G	0045333	biological_process	cellular respiration
G	0099617	cellular_component	matrix side of mitochondrial inner membrane
G	1902600	biological_process	proton transmembrane transport
h	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
h	0045277	cellular_component	respiratory chain complex IV
H	0005739	cellular_component	mitochondrion
H	0005743	cellular_component	mitochondrial inner membrane
H	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
H	0008121	molecular_function	quinol-cytochrome-c reductase activity
H	0009060	biological_process	aerobic respiration
H	0016020	cellular_component	membrane
H	0022904	biological_process	respiratory electron transport chain
H	0045275	cellular_component	respiratory chain complex III
H	0045333	biological_process	cellular respiration
H	1902600	biological_process	proton transmembrane transport
i	0004129	molecular_function	cytochrome-c oxidase activity
i	0005739	cellular_component	mitochondrion
i	0005743	cellular_component	mitochondrial inner membrane
i	0006119	biological_process	oxidative phosphorylation
i	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
i	0016491	molecular_function	oxidoreductase activity
i	0045277	cellular_component	respiratory chain complex IV
i	1902600	biological_process	proton transmembrane transport
I	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
I	0045275	cellular_component	respiratory chain complex III
j	0004129	molecular_function	cytochrome-c oxidase activity
j	0005739	cellular_component	mitochondrion
j	0005743	cellular_component	mitochondrial inner membrane
j	0005758	cellular_component	mitochondrial intermembrane space
j	0006119	biological_process	oxidative phosphorylation
j	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
j	0016491	molecular_function	oxidoreductase activity
j	0031966	cellular_component	mitochondrial membrane
j	0033617	biological_process	mitochondrial respiratory chain complex IV assembly
j	0045277	cellular_component	respiratory chain complex IV
j	0045333	biological_process	cellular respiration
j	1902600	biological_process	proton transmembrane transport
k	0005743	cellular_component	mitochondrial inner membrane
L	0004222	molecular_function	metalloendopeptidase activity
L	0005515	molecular_function	protein binding
L	0005739	cellular_component	mitochondrion
L	0005743	cellular_component	mitochondrial inner membrane
L	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
L	0006627	biological_process	protein processing involved in protein targeting to mitochondrion
L	0008121	molecular_function	quinol-cytochrome-c reductase activity
L	0009060	biological_process	aerobic respiration
L	0017087	cellular_component	mitochondrial processing peptidase complex
L	0022904	biological_process	respiratory electron transport chain
L	0045275	cellular_component	respiratory chain complex III
L	0045333	biological_process	cellular respiration
L	0046872	molecular_function	metal ion binding
L	1902600	biological_process	proton transmembrane transport
M	0004222	molecular_function	metalloendopeptidase activity
M	0005515	molecular_function	protein binding
M	0005739	cellular_component	mitochondrion
M	0005743	cellular_component	mitochondrial inner membrane
M	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
M	0006508	biological_process	proteolysis
M	0008121	molecular_function	quinol-cytochrome-c reductase activity
M	0009060	biological_process	aerobic respiration
M	0016020	cellular_component	membrane
M	0022904	biological_process	respiratory electron transport chain
M	0030061	cellular_component	mitochondrial crista
M	0045275	cellular_component	respiratory chain complex III
M	0045333	biological_process	cellular respiration
M	0046872	molecular_function	metal ion binding
M	1902600	biological_process	proton transmembrane transport
N	0005739	cellular_component	mitochondrion
N	0005743	cellular_component	mitochondrial inner membrane
N	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
N	0008121	molecular_function	quinol-cytochrome-c reductase activity
N	0009055	molecular_function	electron transfer activity
N	0009060	biological_process	aerobic respiration
N	0016020	cellular_component	membrane
N	0016491	molecular_function	oxidoreductase activity
N	0022904	biological_process	respiratory electron transport chain
N	0045275	cellular_component	respiratory chain complex III
N	0045333	biological_process	cellular respiration
N	0046872	molecular_function	metal ion binding
N	1902600	biological_process	proton transmembrane transport
O	0009055	molecular_function	electron transfer activity
O	0020037	molecular_function	heme binding
P	0008121	molecular_function	quinol-cytochrome-c reductase activity
P	0016020	cellular_component	membrane
P	0051537	molecular_function	2 iron, 2 sulfur cluster binding
Q	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
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	0009060	biological_process	aerobic respiration
R	0016020	cellular_component	membrane
R	0022904	biological_process	respiratory electron transport chain
R	0034551	biological_process	mitochondrial respiratory chain complex III assembly
R	0045275	cellular_component	respiratory chain complex III
R	0045333	biological_process	cellular respiration
R	0099617	cellular_component	matrix side of mitochondrial inner membrane
R	1902600	biological_process	proton transmembrane transport
S	0005739	cellular_component	mitochondrion
S	0005743	cellular_component	mitochondrial inner membrane
S	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
S	0008121	molecular_function	quinol-cytochrome-c reductase activity
S	0009060	biological_process	aerobic respiration
S	0016020	cellular_component	membrane
S	0022904	biological_process	respiratory electron transport chain
S	0045275	cellular_component	respiratory chain complex III
S	0045333	biological_process	cellular respiration
S	1902600	biological_process	proton transmembrane transport
T	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
T	0045275	cellular_component	respiratory chain complex III
U	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
V	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue CU a 601

Chain	Residue
a	HIS241
a	HIS290
a	HIS291
a	HEA603

site_id	AC2
Number of Residues	27
Details	binding site for residue HEA a 602

Chain	Residue
a	VAL59
a	HIS62
a	ALA63
a	MET66
a	VAL71
a	TYR371
a	VAL374
a	PHE377
a	HIS378
a	LEU381
a	SER382
a	LEU389
a	PHE390
a	PHE425
a	MET428
a	ARG438
a	ARG439
a	SER458
a	ALA461
a	LEU465
a	PHE468
a	HEA603
a	PHE19
a	THR30
a	SER33
a	ILE36
a	ARG37

site_id	AC3
Number of Residues	21
Details	binding site for residue HEA a 603

Chain	Residue
a	TRP127
a	TRP237
a	VAL244
a	TYR245
a	HIS290
a	HIS291
a	ILE312
a	ALA313
a	GLY352
a	GLY355
a	LEU358
a	ALA359
a	ASP364
a	HIS368
a	HIS376
a	PHE377
a	VAL380
a	LEU381
a	ARG438
a	CU601
a	HEA602

site_id	AC4
Number of Residues	10
Details	binding site for residue PTY a 604

Chain	Residue
a	PHE95
a	PRO96
a	ARG97
a	ILE98
c	TRP65
c	ILE69
c	ILE87
c	PHE91
c	PHE94
c	PTY301

site_id	AC5
Number of Residues	7
Details	binding site for residue CN3 a 605

Chain	Residue
H	LYS35
a	ASN406
a	LYS408
a	PHE466
a	TYR470
a	LYS487
e	PHE94

site_id	AC6
Number of Residues	7
Details	binding site for residue CUA b 301

Chain	Residue
b	HIS186
b	CYS221
b	GLU223
b	LEU224
b	CYS225
b	HIS229
b	MET232

site_id	AC7
Number of Residues	7
Details	binding site for residue PTY b 302

Chain	Residue
a	LEU339
a	ILE342
a	TRP415
b	THR60
b	ILE61
b	VAL62
e	SER92

site_id	AC8
Number of Residues	18
Details	binding site for residue PTY c 301

Chain	Residue
c	GLY242
c	THR245
a	PTY604
c	LEU59
c	PHE66
c	ALA73
c	THR74
c	PHE91
c	VAL217
c	MET218
c	ALA221
c	MET222
c	ARG229
c	HIS234
c	LEU235
c	HIS239
c	HIS240
c	VAL241

site_id	AC9
Number of Residues	12
Details	binding site for residue PCF c 302

Chain	Residue
a	SER204
c	GLU188
c	TYR189
c	THR190
c	ALA192
c	PHE194
c	THR195
c	ILE196
c	TYR206
k	THR114
k	LEU115
k	ASN122

site_id	AD1
Number of Residues	4
Details	binding site for residue ZN d 201

Chain	Residue
d	CYS111
d	HIS119
d	CYS134
d	CYS137

site_id	AD2
Number of Residues	7
Details	binding site for residue PCF e 201

Chain	Residue
D	PTY402
a	TYR452
e	ALA111
e	ARG114
e	MET115
e	GLY118
m	PCF103

site_id	AD3
Number of Residues	7
Details	binding site for residue PTY i 101

Chain	Residue
a	LEU324
b	MET57
b	GLY78
b	ILE81
i	LYS11
i	VAL14
i	ILE15

site_id	AD4
Number of Residues	16
Details	binding site for residue PTY m 101

Chain	Residue
a	THR354
a	HIS429
a	PHE430
b	THR19
b	PRO20
b	TYR21
b	ALA22
b	CYS23
b	MET44
b	LEU51
i	PHE36
m	LEU51
m	PRO54
m	GLY55
m	TYR58
m	PTY102

site_id	AD5
Number of Residues	6
Details	binding site for residue PTY m 102

Chain	Residue
i	TYR31
i	TRP32
m	LEU47
m	LEU51
m	GLY52
m	PTY101

site_id	AD6
Number of Residues	6
Details	binding site for residue PCF m 103

Chain	Residue
a	TYR452
b	TYR21
e	PCF201
m	VAL57
m	PHE60
m	SER61

site_id	AD7
Number of Residues	6
Details	binding site for residue 6PH C 401

Chain	Residue
C	GLY37
C	HIS222
C	SER223
C	PHE227
C	LEU230
I	PCF101

site_id	AD8
Number of Residues	18
Details	binding site for residue HEM C 402

Chain	Residue
C	LEU40
C	GLN43
C	GLY47
C	ILE48
C	MET50
C	VAL65
C	ARG79
C	HIS82
C	ALA83
C	ALA86
C	ALA128
C	GLY131
C	TYR132
C	VAL135
C	HIS183
C	TYR184
C	PRO187
C	TYR274

site_id	AD9
Number of Residues	15
Details	binding site for residue HEM C 403

Chain	Residue
C	TRP30
C	GLY33
C	PHE89
C	HIS96
C	MET97
C	LYS99
C	SER105
C	LEU113
C	GLY117
C	ILE120
C	HIS197
C	LEU201
C	SER206
C	SER207
C	UQ6406

site_id	AE1
Number of Residues	11
Details	binding site for residue 8PE C 404

Chain	Residue
C	TRP29
C	PHE94
C	ALA98
C	TYR102
C	TYR103
C	PHE121
C	THR317
C	PHE327
C	PHE331
C	PHE333
C	TYR359

site_id	AE2
Number of Residues	7
Details	binding site for residue CN5 C 405

Chain	Residue
C	LEU12
C	TYR16
C	MET199
N	LEU12
N	TYR16
N	ILE195
N	MET199

site_id	AE3
Number of Residues	8
Details	binding site for residue UQ6 C 406

Chain	Residue
C	TYR16
C	ILE17
C	SER34
C	VAL41
C	PHE49
C	LEU201
C	MET221
C	HEM403

site_id	AE4
Number of Residues	2
Details	binding site for residue 9PE C 407

Chain	Residue
C	ASN7
N	ASN115

site_id	AE5
Number of Residues	12
Details	binding site for residue HEM D 401

Chain	Residue
D	VAL100
D	CYS101
D	CYS104
D	HIS105
D	ASN169
D	PRO175
D	ILE180
D	ARG184
D	TYR190
D	PHE218
D	MET225
D	VAL228

site_id	AE6
Number of Residues	5
Details	binding site for residue PTY D 402

Chain	Residue
D	PHE82
D	LEU271
I	TRP39
I	HIS43
e	PCF201

site_id	AE7
Number of Residues	7
Details	binding site for residue 7PH E 301

Chain	Residue
D	LEU269
D	LYS272
D	THR273
E	GLY70
E	SER73
E	GLU76
E	THR77

site_id	AE8
Number of Residues	8
Details	binding site for residue FES E 302

Chain	Residue
E	CYS159
E	LEU162
E	CYS164
E	CYS178
E	CYS180
E	HIS181
E	SER183
E	TYR185

site_id	AE9
Number of Residues	9
Details	binding site for residue PCF I 101

Chain	Residue
A	ASP428
C	6PH401
E	TYR57
E	SER67
I	PHE11
I	LYS12
I	ASN14
I	PHE17
I	VAL18

site_id	AF1
Number of Residues	14
Details	binding site for residue HEM N 401

Chain	Residue
N	LEU40
N	GLN43
N	GLY47
N	MET50
N	ALA51
N	ARG79
N	HIS82
N	ALA86
N	GLY131
N	TYR132
N	HIS183
N	TYR184
N	PRO187
N	TYR274

site_id	AF2
Number of Residues	14
Details	binding site for residue HEM N 402

Chain	Residue
N	TRP30
N	GLY33
N	HIS96
N	MET97
N	LYS99
N	SER105
N	LEU113
N	GLY117
N	ILE120
N	HIS197
N	LEU201
N	SER206
N	SER207
N	UQ6403

site_id	AF3
Number of Residues	9
Details	binding site for residue UQ6 N 403

Chain	Residue
N	TYR16
N	SER34
N	GLY37
N	ILE44
N	PHE49
N	VAL194
N	MET221
N	ASP229
N	HEM402

site_id	AF4
Number of Residues	9
Details	binding site for residue 8PE N 404

Chain	Residue
N	TRP29
N	PHE94
N	MET95
N	TYR102
N	TYR103
N	THR317
N	PHE331
N	PHE333
S	GLN55

site_id	AF5
Number of Residues	5
Details	binding site for residue 9PE N 405

Chain	Residue
C	THR112
C	ASN115
N	PHE3
N	ASN7
N	TYR9

site_id	AF6
Number of Residues	9
Details	binding site for residue CN3 N 406

Chain	Residue
N	ASN27
N	TYR28
N	MET32
O	TYR281
O	ILE285
O	LYS288
O	LYS289
R	HIS85
S	ARG51

site_id	AF7
Number of Residues	7
Details	binding site for residue 6PH O 401

Chain	Residue
L	MET455
N	HIS222
N	PHE227
N	LEU230
N	PHE234
O	LYS291
T	PCF101

site_id	AF8
Number of Residues	13
Details	binding site for residue HEM O 402

Chain	Residue
O	VAL100
O	CYS101
O	CYS104
O	HIS105
O	PRO174
O	ILE180
O	ARG184
O	TYR190
O	LEU195
O	PHE218
O	ALA224
O	MET225
O	VAL228

site_id	AF9
Number of Residues	8
Details	binding site for residue 7PH O 403

Chain	Residue
N	MET237
N	PHE245
O	LEU269
O	LYS272
O	THR273
P	GLY70
P	SER73
P	PHE78

site_id	AG1
Number of Residues	8
Details	binding site for residue FES P 301

Chain	Residue
P	CYS159
P	HIS161
P	LEU162
P	CYS164
P	CYS178
P	HIS181
P	SER183
P	TYR185

site_id	AG2
Number of Residues	11
Details	binding site for residue PCF T 101

Chain	Residue
L	ASP428
O	6PH401
P	TYR57
P	SER67
P	SER68
T	PHE11
T	LYS12
T	ASN14
T	PHE17
T	VAL18
T	ILE21

Functional Information from PROSITE/UniProt

site_id	PS00077
Number of Residues	55
Details	COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyiliipgfgiishvvstyskkpvfgeismvyamasigllgflvws..HH

Chain	Residue	Details
a	TRP237-HIS291

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

Chain	Residue	Details
b	VAL184-MET232

site_id	PS00143
Number of Residues	23
Details	INSULINASE Insulinase family, zinc-binding region signature. Ggsryatkd.GvAHLLNRFnFqNT

Chain	Residue	Details
B	GLY37-THR59

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

Chain	Residue	Details
d	ILE121-LEU143

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

Chain	Residue	Details
k	ILE101-ASN118

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	75
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	336
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	86
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	156
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	53
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	51
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	54
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	62
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	41
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	28
Details	Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	29
Details	Transmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598556","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598556","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17215247","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17761666","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	174
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	3
Details	Propeptide: {"featureId":"PRO_0000006174","evidences":[{"source":"PubMed","id":"6327685","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	43
Details	Domain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
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_FI27
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_FI28
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17761666","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	162
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8031140","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	366
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	208
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8031140","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	8
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KB9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P84","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IBZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PD4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00157","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	400
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9430684","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	234
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	24
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9430684","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	306
Details	Domain: {"description":"Cytochrome c","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	74
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	18
Details	Compositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	4
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI43
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI44
Number of Residues	132
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI45
Number of Residues	294
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI46
Number of Residues	182
Details	Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI47
Number of Residues	6
Details	Region: {"description":"Hinge","evidences":[{"source":"PubMed","id":"30598556","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI48
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10873857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30598554","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EZV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KB9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P84","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IBZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PD4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI49
Number of Residues	20
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	1
Details	M-CSA 208

Chain	Residue	Details
O	HIS263	electrostatic stabiliser, hydrogen bond donor, radical stabiliser
O	LYS267	electrostatic stabiliser, hydrogen bond donor, radical stabiliser
O	LYS289	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser
O	PHE290	electrostatic stabiliser, hydrogen bond acceptor, radical stabiliser

site_id	MCSA2
Number of Residues	1
Details	M-CSA 208

Chain

Residue

Details

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