Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5WAU

Crystal Structure of CO-bound Cytochrome c Oxidase determined by Synchrotron X-Ray Crystallography at 100 K

Functional Information from GO Data

Chain	GOid	namespace	contents
a	0004129	molecular_function	cytochrome-c oxidase activity
a	0005743	cellular_component	mitochondrial inner membrane
a	0006119	biological_process	oxidative phosphorylation
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	0045277	cellular_component	respiratory chain complex IV
a	0046872	molecular_function	metal ion binding
a	1902600	biological_process	proton transmembrane transport
A	0004129	molecular_function	cytochrome-c oxidase activity
A	0005743	cellular_component	mitochondrial inner membrane
A	0006119	biological_process	oxidative phosphorylation
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	0045277	cellular_component	respiratory chain complex IV
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	0005739	cellular_component	mitochondrion
b	0005743	cellular_component	mitochondrial inner membrane
b	0016020	cellular_component	membrane
b	0016491	molecular_function	oxidoreductase activity
b	0017004	biological_process	cytochrome complex assembly
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	0004129	molecular_function	cytochrome-c oxidase activity
B	0005507	molecular_function	copper ion binding
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0017004	biological_process	cytochrome complex assembly
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
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	0008535	biological_process	respiratory chain complex IV assembly
c	0009055	molecular_function	electron transfer activity
c	0016020	cellular_component	membrane
c	0019646	biological_process	aerobic electron transport chain
c	0022904	biological_process	respiratory electron transport chain
c	0045277	cellular_component	respiratory chain complex IV
c	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	0008535	biological_process	respiratory chain complex IV assembly
C	0009055	molecular_function	electron transfer activity
C	0016020	cellular_component	membrane
C	0019646	biological_process	aerobic electron transport chain
C	0022904	biological_process	respiratory electron transport chain
C	0045277	cellular_component	respiratory chain complex IV
C	1902600	biological_process	proton transmembrane transport
d	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
d	0045277	cellular_component	respiratory chain complex IV
D	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
D	0045277	cellular_component	respiratory chain complex IV
e	0005743	cellular_component	mitochondrial inner membrane
e	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
e	0045277	cellular_component	respiratory chain complex IV
E	0005743	cellular_component	mitochondrial inner membrane
E	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
E	0045277	cellular_component	respiratory chain complex IV
f	0005740	cellular_component	mitochondrial envelope
f	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
f	0045277	cellular_component	respiratory chain complex IV
F	0005740	cellular_component	mitochondrial envelope
F	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
F	0045277	cellular_component	respiratory chain complex IV
g	0005743	cellular_component	mitochondrial inner membrane
G	0005743	cellular_component	mitochondrial inner membrane
h	0005739	cellular_component	mitochondrion
h	0005743	cellular_component	mitochondrial inner membrane
h	0006119	biological_process	oxidative phosphorylation
h	0016020	cellular_component	membrane
h	0045277	cellular_component	respiratory chain complex IV
H	0005739	cellular_component	mitochondrion
H	0005743	cellular_component	mitochondrial inner membrane
H	0006119	biological_process	oxidative phosphorylation
H	0016020	cellular_component	membrane
H	0045277	cellular_component	respiratory chain complex IV
i	0005743	cellular_component	mitochondrial inner membrane
i	0006119	biological_process	oxidative phosphorylation
i	0016020	cellular_component	membrane
i	0045277	cellular_component	respiratory chain complex IV
I	0005743	cellular_component	mitochondrial inner membrane
I	0006119	biological_process	oxidative phosphorylation
I	0016020	cellular_component	membrane
I	0045277	cellular_component	respiratory chain complex IV
j	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
j	0045277	cellular_component	respiratory chain complex IV
J	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
J	0045277	cellular_component	respiratory chain complex IV
k	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
K	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
l	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
l	0045277	cellular_component	respiratory chain complex IV
L	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
L	0045277	cellular_component	respiratory chain complex IV
m	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
m	0045277	cellular_component	respiratory chain complex IV
M	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
M	0045277	cellular_component	respiratory chain complex IV

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	binding site for residue HEA A 601

Chain	Residue
A	MET28
A	MET65
A	VAL70
A	ILE73
A	GLY125
A	TRP126
A	TYR371
A	PHE377
A	HIS378
A	LEU381
A	MET417
A	THR31
A	PHE425
A	GLN428
A	ARG438
A	ARG439
A	VAL465
A	HOH717
A	HOH737
A	HOH782
A	SER34
A	ILE37
A	ARG38
A	TYR54
A	VAL58
A	HIS61
A	ALA62

site_id	AC2
Number of Residues	28
Details	binding site for residue HEA A 602

Chain	Residue
A	TRP126
A	TRP236
A	VAL243
A	TYR244
A	HIS290
A	THR309
A	ILE312
A	THR316
A	GLY317
A	GLY352
A	GLY355
A	ILE356
A	LEU358
A	ALA359
A	ASP364
A	HIS368
A	VAL373
A	HIS376
A	PHE377
A	VAL380
A	LEU381
A	ARG438
A	CMO610
A	HOH711
A	HOH712
A	HOH716
A	HOH721
B	ILE34

site_id	AC3
Number of Residues	4
Details	binding site for residue CU A 603

Chain	Residue
A	HIS240
A	HIS290
A	HIS291
A	CMO610

site_id	AC4
Number of Residues	6
Details	binding site for residue MG A 604

Chain	Residue
A	HIS368
A	ASP369
B	GLU198
B	HOH529
B	HOH540
B	HOH610

site_id	AC5
Number of Residues	4
Details	binding site for residue NA A 605

Chain	Residue
A	GLU40
A	GLY45
A	SER441
A	HOH835

site_id	AC6
Number of Residues	14
Details	binding site for residue PGV A 606

Chain	Residue
A	ASN406
A	THR408
A	TRP409
A	HOH701
A	HOH743
A	HOH848
A	HOH880
D	PHE87
D	PHE91
K	ASP8
K	PHE9
M	GLN15
M	ALA16
M	LEU19

site_id	AC7
Number of Residues	14
Details	binding site for residue PGV A 607

Chain	Residue
A	PHE94
A	PRO95
A	ARG96
A	MET97
A	HOH731
C	HIS9
C	ALA24
C	ASN50
C	MET54
C	TRP57
C	TRP58
C	GLU64
C	HIS71
C	GLY82

site_id	AC8
Number of Residues	7
Details	binding site for residue TGL A 608

Chain	Residue
A	HOH892
B	LEU28
B	SER35
D	HOH419
I	ARG43
A	PHE430
A	LEU433

site_id	AC9
Number of Residues	11
Details	binding site for residue TGL A 609

Chain	Residue
A	PHE2
A	LEU18
A	PHE400
L	ILE11
L	PRO12
L	PHE13
L	ARG20
L	MET24
L	PHE28
L	PHE29
L	HOH116

site_id	AD1
Number of Residues	6
Details	binding site for residue CMO A 610

Chain	Residue
A	HIS240
A	VAL243
A	HIS290
A	HIS291
A	HEA602
A	CU603

site_id	AD2
Number of Residues	6
Details	binding site for residue FME B 301

Chain	Residue
B	ALA2
B	GLN10
B	LEU133
B	TYR192
B	TYR193
D	VAL128

site_id	AD3
Number of Residues	6
Details	binding site for residue CUA B 401

Chain	Residue
B	HIS161
B	CYS196
B	GLU198
B	CYS200
B	HIS204
B	MET207

site_id	AD4
Number of Residues	12
Details	binding site for residue CHD B 402

Chain	Residue
A	MET271
B	GLU62
B	THR63
B	HOH518
B	HOH521
B	HOH534
B	HOH545
B	HOH566
c	PEK305
g	ARG14
g	ARG17
g	GLY22

site_id	AD5
Number of Residues	12
Details	binding site for residue CHD C 301

Chain	Residue
A	HIS233
A	ASP300
A	THR301
A	TYR304
C	TRP99
C	HIS103
C	PGV304
C	HOH474
C	HOH487
C	HOH488
C	HOH494
g	CDL101

site_id	AD6
Number of Residues	15
Details	binding site for residue PEK C 302

Chain	Residue
A	VAL155
C	TYR181
C	TYR182
C	ALA184
C	PHE186
C	THR187
C	ILE188
C	PHE198
C	PHE203
C	HOH456
G	THR68
G	PHE69
G	PHE70
G	HIS71
G	ASN76

site_id	AD7
Number of Residues	14
Details	binding site for residue PGV C 303

Chain	Residue
C	VAL61
C	SER65
C	THR66
C	ILE210
C	PHE214
C	ARG221
C	HIS226
C	PHE227
C	HIS231
C	PHE233
C	GLY234
C	HOH406
C	HOH418
C	HOH440

site_id	AD8
Number of Residues	12
Details	binding site for residue PGV C 304

Chain	Residue
A	ASP298
C	TRP99
C	HIS103
C	LEU106
C	ALA107
C	CHD301
C	HOH419
C	HOH422
H	ASN22
c	TRP258
c	TRP259
g	ALA1

site_id	AD9
Number of Residues	12
Details	binding site for residue CDL C 305

Chain	Residue
C	MET51
C	TYR55
C	ARG59
C	ARG63
C	PHE67
C	ILE216
C	VAL217
C	PHE220
C	LYS224
C	HIS226
C	HOH475
J	LYS8

site_id	AE1
Number of Residues	6
Details	binding site for residue CHD C 306

Chain	Residue
C	ARG156
C	PHE164
C	LEU223
C	HOH454
C	HOH489
J	PHE1

site_id	AE2
Number of Residues	8
Details	binding site for residue PEK C 307

Chain	Residue
C	LYS77
C	ARG80
C	TYR81
C	VAL91
C	PHE98
C	TRP240
C	VAL247
C	PHE251

site_id	AE3
Number of Residues	5
Details	binding site for residue DMU C 308

Chain	Residue
C	TRP34
C	MET40
C	HOH415
G	TRP62
G	GLY63

site_id	AE4
Number of Residues	9
Details	binding site for residue TGL D 201

Chain	Residue
A	TRP334
A	MET339
B	LEU39
B	LEU46
B	THR47
D	TRP78
D	HOH301
D	HOH303
D	HOH323

site_id	AE5
Number of Residues	10
Details	binding site for residue PSC E 201

Chain	Residue
A	HIS328
B	HIS52
B	MET56
B	ASP57
B	GLU60
B	TRP65
E	ASP8
E	PHE11
E	LEU41
I	ARG10

site_id	AE6
Number of Residues	4
Details	binding site for residue ZN F 101

Chain	Residue
F	CYS60
F	CYS62
F	CYS82
F	CYS85

site_id	AE7
Number of Residues	9
Details	binding site for residue PEK G 101

Chain	Residue
C	LYS157
C	HIS158
C	GLN161
C	THR168
C	TYR172
G	ARG17
G	PHE21
G	CHD103
b	GLN59

site_id	AE8
Number of Residues	17
Details	binding site for residue CDL G 102

Chain	Residue
C	LEU131
C	PHE251
G	SER27
G	CYS31
G	ASN34
G	LEU37
G	HIS38
G	HOH202
G	HOH231
a	ASP300
a	TYR304
a	SER307
a	ILE311
b	ALA77
b	LEU78
b	LEU81
c	PEK301

site_id	AE9
Number of Residues	11
Details	binding site for residue CHD G 103

Chain	Residue
G	ARG14
G	ARG17
G	GLY22
G	PEK101
G	HOH204
G	HOH211
G	HOH217
G	HOH225
a	MET271
b	GLU62
b	THR63

site_id	AF1
Number of Residues	5
Details	binding site for residue SAC I 101

Chain	Residue
I	THR2
e	PRO77
e	HIS78
e	LYS79
e	GLU80

site_id	AF2
Number of Residues	4
Details	binding site for residue CHD J 101

Chain	Residue
J	ARG33
J	MET36
J	THR37
J	LEU40

site_id	AF3
Number of Residues	6
Details	binding site for residue DMU M 101

Chain	Residue
D	TRP98
M	LEU27
M	LEU28
M	TRP32
M	TYR35
M	HIS36

site_id	AF4
Number of Residues	25
Details	binding site for residue HEA a 601

Chain	Residue
a	THR31
a	SER34
a	ILE37
a	ARG38
a	TYR54
a	VAL58
a	HIS61
a	ALA62
a	MET65
a	ILE66
a	VAL70
a	ILE73
a	GLY125
a	TRP126
a	TYR371
a	PHE377
a	HIS378
a	SER382
a	PHE425
a	GLN428
a	ARG438
a	ARG439
a	VAL465
a	HOH721
a	HOH774

site_id	AF5
Number of Residues	28
Details	binding site for residue HEA a 602

Chain	Residue
a	TRP126
a	TRP236
a	VAL243
a	TYR244
a	HIS290
a	HIS291
a	THR309
a	ILE312
a	THR316
a	GLY317
a	GLY352
a	GLY355
a	ILE356
a	LEU358
a	ALA359
a	ASP364
a	HIS368
a	VAL373
a	HIS376
a	PHE377
a	VAL380
a	LEU381
a	ARG438
a	CMO608
a	HOH755
a	HOH781
a	HOH822
a	HOH846

site_id	AF6
Number of Residues	4
Details	binding site for residue CU a 603

Chain	Residue
a	HIS240
a	HIS290
a	HIS291
a	CMO608

site_id	AF7
Number of Residues	5
Details	binding site for residue MG a 604

Chain	Residue
a	HIS368
a	ASP369
b	GLU198
b	HOH416
b	HOH426

site_id	AF8
Number of Residues	4
Details	binding site for residue NA a 605

Chain	Residue
a	GLU40
a	GLY45
a	SER441
a	HOH831

site_id	AF9
Number of Residues	11
Details	binding site for residue PGV a 606

Chain	Residue
a	ASN406
a	THR408
a	TRP409
d	PHE91
k	PHE9
k	HIS10
m	PRO9
m	THR10
m	SER11
m	GLN15
m	HOH205

site_id	AG1
Number of Residues	15
Details	binding site for residue PGV a 607

Chain	Residue
a	PHE94
a	PRO95
a	ARG96
a	MET97
a	PHE148
a	HOH783
c	HIS9
c	ASN50
c	TRP57
c	TRP58
c	GLU64
c	HIS71
c	LEU79
c	GLY82
c	GLU90

site_id	AG2
Number of Residues	5
Details	binding site for residue CMO a 608

Chain	Residue
a	HIS240
a	VAL243
a	HIS291
a	HEA602
a	CU603

site_id	AG3
Number of Residues	6
Details	binding site for residue CUA b 301

Chain	Residue
b	HIS161
b	CYS196
b	GLU198
b	CYS200
b	HIS204
b	MET207

site_id	AG4
Number of Residues	8
Details	binding site for residue TGL b 302

Chain	Residue
a	ASN422
a	PHE426
a	LEU433
b	HIS24
b	LEU28
b	PHE32
b	SER35
i	ARG43

site_id	AG5
Number of Residues	13
Details	binding site for residue PSC b 303

Chain	Residue
a	PHE321
a	LEU324
a	HOH830
b	ILE41
b	MET56
b	ASP57
b	VAL61
b	ILE64
b	TRP65
e	GLU6
e	ASP8
e	HOH230
i	ARG10

site_id	AG6
Number of Residues	7
Details	binding site for residue PEK c 301

Chain	Residue
G	TPO11
G	CDL102
c	ILE84
c	TRP240
c	VAL247
c	HOH416
c	HOH423

site_id	AG7
Number of Residues	7
Details	binding site for residue PGV c 302

Chain	Residue
C	TRP258
c	THR95
c	TRP99
c	ALA107
c	CHD303
c	HOH401
c	HOH414

site_id	AG8
Number of Residues	8
Details	binding site for residue CHD c 303

Chain	Residue
a	HIS233
a	ASP300
a	THR301
a	TYR304
a	HOH746
c	TRP99
c	HIS103
c	PGV302

site_id	AG9
Number of Residues	16
Details	binding site for residue PEK c 304

Chain	Residue
a	HIS151
a	VAL155
c	TYR181
c	TYR182
c	ALA184
c	PHE186
c	THR187
c	ILE188
c	PHE198
c	HOH433
g	TRP62
g	THR68
g	PHE69
g	PHE70
g	HIS71
g	ASN76

site_id	AH1
Number of Residues	9
Details	binding site for residue PEK c 305

Chain	Residue
B	GLN59
B	THR66
B	CHD402
B	HOH566
c	LYS157
c	HIS158
f	ALA1
g	ARG17
g	PHE21

site_id	AH2
Number of Residues	18
Details	binding site for residue PGV c 306

Chain	Residue
c	VAL61
c	SER65
c	THR66
c	LEU79
c	MET83
c	ILE210
c	PHE214
c	ARG221
c	HIS226
c	PHE227
c	HIS231
c	HIS232
c	PHE233
c	GLY234
c	CDL307
c	HOH415
c	HOH418
c	HOH439

site_id	AH3
Number of Residues	7
Details	binding site for residue CDL c 307

Chain	Residue
c	TYR55
c	ARG59
c	PHE67
c	HIS226
c	PGV306
c	HOH475
j	LYS8

site_id	AH4
Number of Residues	6
Details	binding site for residue CHD c 308

Chain	Residue
c	ARG156
c	PHE164
c	LEU223
c	HOH413
c	HOH430
j	PHE1

site_id	AH5
Number of Residues	7
Details	binding site for residue DMU c 309

Chain	Residue
c	TRP34
c	ASN38
c	THR41
c	HOH410
c	HOH438
g	TRP62
g	GLY63

site_id	AH6
Number of Residues	8
Details	binding site for residue TGL d 201

Chain	Residue
a	TRP334
a	MET339
a	GLY343
d	ARG73
d	THR75
d	GLU77
d	TRP78
i	ARG16

site_id	AH7
Number of Residues	4
Details	binding site for residue ZN f 101

Chain	Residue
f	CYS60
f	CYS62
f	CYS82
f	CYS85

site_id	AH8
Number of Residues	16
Details	binding site for residue CDL g 101

Chain	Residue
A	SER307
A	ILE311
B	HOH530
C	CHD301
c	ASN125
c	LEU127
c	LEU131
c	THR134
c	HOH495
g	SER27
g	CYS31
g	ASN34
g	LEU37
g	HIS38
g	HOH214
g	HOH216

site_id	AH9
Number of Residues	5
Details	binding site for residue CHD j 101

Chain	Residue
a	HOH811
j	TYR32
j	ARG33
j	THR37
j	LEU40

site_id	AI1
Number of Residues	13
Details	binding site for residue TGL l 101

Chain	Residue
a	PHE2
a	THR17
a	LEU18
a	LEU21
a	TRP25
a	LEU113
a	PHE400
l	ILE11
l	PRO12
l	PHE13
l	MET24
l	PHE28
l	PHE29

site_id	AI2
Number of Residues	9
Details	binding site for residue DMU m 101

Chain	Residue
a	PHE459
d	LEU95
d	TRP98
l	PHE37
m	LEU27
m	LEU28
m	TRP32
m	TYR35
m	HIS36

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
A	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
B	VAL159-MET207

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

Chain	Residue	Details
F	VAL69-LEU91

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

Chain	Residue	Details
G	ILE55-ASN72

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	152
Details	Transmembrane: {"description":"Helical; Name=I","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	18
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_FI3
Number of Residues	174
Details	Transmembrane: {"description":"Helical; Name=II","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	60
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_FI5
Number of Residues	108
Details	Transmembrane: {"description":"Helical; Name=III","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	94
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_FI7
Number of Residues	104
Details	Transmembrane: {"description":"Helical; Name=IV","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	112
Details	Transmembrane: {"description":"Helical; Name=V","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	130
Details	Transmembrane: {"description":"Helical; Name=VI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	78
Details	Transmembrane: {"description":"Helical; Name=VII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	56
Details	Transmembrane: {"description":"Helical; Name=VIII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	138
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	42
Details	Transmembrane: {"description":"Helical; Name=IX","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	214
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	58
Details	Transmembrane: {"description":"Helical; Name=X","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	52
Details	Transmembrane: {"description":"Helical; Name=XI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	62
Details	Transmembrane: {"description":"Helical; Name=XII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	6
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_FI19
Number of Residues	6
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_FI20
Number of Residues	22
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_FI21
Number of Residues	2
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	4
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_FI23
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00406","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	384
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P13073","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10888","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P12787","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P20674","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	8
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_FI32
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19536","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	92
Details	Domain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	20
Details	Motif: {"description":"Cx9C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	22
Details	Motif: {"description":"Cx10C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56391","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17665","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	14
Details	M-CSA 124

Chain	Residue	Details
A	MET65	metal ligand
A	THR294	metal ligand
A	VAL295	metal ligand, proton acceptor, proton donor
A	VAL320	proton acceptor, proton donor, proton relay
A	TRP323	proton acceptor, proton donor, proton relay
A	ASP442	proton acceptor, proton donor, proton relay
A	PRO95	proton acceptor, proton donor, proton relay
A	PRO130	proton acceptor, proton donor, proton relay
A	GLY160	proton acceptor, proton donor, proton relay
A	ALA161	proton acceptor, proton donor, proton relay
A	TYR244	covalently attached, electrostatic stabiliser, metal ligand, radical stabiliser
A	LEU246	proton acceptor, proton donor, proton relay
A	LEU248	covalently attached, hydrogen radical donor, proton acceptor, proton donor, proton relay, single electron acceptor
A	THR259	proton acceptor, proton donor, proton relay

site_id	MCSA2
Number of Residues	14
Details	M-CSA 124

Chain

Residue

Details

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