Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5W97

Crystal Structure of CO-bound Cytochrome c Oxidase determined by Serial Femtosecond X-Ray Crystallography at Room Temperature

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	THR31
A	VAL70
A	GLY125
A	TRP126
A	TYR371
A	PHE377
A	HIS378
A	SER382
A	MET390
A	MET417
A	PHE425
A	SER34
A	GLN428
A	ARG438
A	ARG439
A	VAL465
A	MET468
A	HOH724
A	HOH726
A	HOH747
A	ILE37
A	ARG38
A	TYR54
A	HIS61
A	ALA62
A	MET65
A	ILE66

site_id	AC2
Number of Residues	26
Details	binding site for residue HEA A 602

Chain	Residue
A	TRP126
A	TRP236
A	VAL243
A	TYR244
A	ILE247
A	HIS290
A	HIS291
A	THR309
A	ILE312
A	GLY317
A	GLY352
A	GLY355
A	LEU358
A	ALA359
A	ASP364
A	HIS368
A	VAL373
A	HIS376
A	PHE377
A	VAL380
A	ARG438
A	CMO609
A	HOH707
A	HOH758
A	HOH785
A	HOH837

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

Chain	Residue
A	HIS240
A	HIS290
A	HIS291
A	CMO609

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

Chain	Residue
A	HIS368
A	ASP369
B	GLU198
B	HOH419
B	HOH421
B	HOH486

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

Chain	Residue
A	GLU40
A	GLY45
A	SER441
A	HOH826

site_id	AC6
Number of Residues	6
Details	binding site for residue PGV A 606

Chain	Residue
A	TRP409
A	HOH701
A	HOH765
A	HOH790
D	THR80
M	GLN15

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	HOH745
C	HIS9
C	ASN50
C	MET54
C	TRP57
C	TRP58
C	GLU64
C	HIS71
C	PHE86
C	PEK302

site_id	AC8
Number of Residues	8
Details	binding site for residue TGL A 608

Chain	Residue
A	VAL350
A	ASN422
A	PHE426
A	PHE430
A	LEU433
B	GLY8
B	LEU28
I	ARG43

site_id	AC9
Number of Residues	5
Details	binding site for residue CMO A 609

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

site_id	AD1
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	AD2
Number of Residues	7
Details	binding site for residue PSC B 302

Chain	Residue
B	HIS52
B	ASP57
B	GLU60
B	HOH467
E	ASP8
E	LEU41
I	ARG18

site_id	AD3
Number of Residues	9
Details	binding site for residue CHD B 303

Chain	Residue
A	MET271
B	GLN59
B	GLU62
B	THR63
B	HOH414
B	HOH442
g	ARG14
g	ARG17
g	GLY22

site_id	AD4
Number of Residues	8
Details	binding site for residue CHD C 301

Chain	Residue
A	ASP300
A	THR301
A	TYR304
A	HOH845
C	TRP99
C	HIS103
C	HOH453
g	CDL103

site_id	AD5
Number of Residues	14
Details	binding site for residue PEK C 302

Chain	Residue
A	PGV607
C	TYR181
C	TYR182
C	ALA184
C	PHE186
C	THR187
C	ILE188
C	PHE198
G	TRP62
G	THR68
G	PHE69
G	PHE70
G	HIS71
G	ASN76

site_id	AD6
Number of Residues	15
Details	binding site for residue PGV C 303

Chain	Residue
C	MET54
C	VAL61
C	SER65
C	THR66
C	ILE210
C	ARG221
C	HIS226
C	HIS231
C	HIS232
C	PHE233
C	GLY234
C	CDL305
C	HOH423
C	HOH443
F	HOH237

site_id	AD7
Number of Residues	6
Details	binding site for residue PGV C 304

Chain	Residue
A	ASP298
C	TYR102
C	HIS103
C	ALA107
H	ASN22
g	ALA1

site_id	AD8
Number of Residues	12
Details	binding site for residue CDL C 305

Chain	Residue
C	MET54
C	TYR55
C	ARG63
C	PHE67
C	VAL217
C	LYS224
C	HIS226
C	PGV303
C	HOH414
C	HOH446
J	PHE12
J	ASP28

site_id	AD9
Number of Residues	3
Details	binding site for residue CHD C 306

Chain	Residue
C	ARG156
C	PHE164
J	PHE1

site_id	AE1
Number of Residues	5
Details	binding site for residue DMU C 307

Chain	Residue
C	ASN38
C	MET40
C	HOH461
G	TRP62
G	GLY63

site_id	AE2
Number of Residues	7
Details	binding site for residue PEK C 308

Chain	Residue
C	LYS157
G	ARG17
G	GLY22
G	CDL101
G	HOH242
b	THR66
b	CHD301

site_id	AE3
Number of Residues	10
Details	binding site for residue PEK C 309

Chain	Residue
C	LYS77
C	ARG80
C	TYR81
C	ILE84
C	VAL91
C	TRP240
C	VAL247
C	PHE251
g	HIS8
g	TPO11

site_id	AE4
Number of Residues	5
Details	binding site for residue TGL D 201

Chain	Residue
A	TRP334
A	LYS411
D	TRP78
D	HOH328
I	ARG16

site_id	AE5
Number of Residues	4
Details	binding site for residue ZN F 101

Chain	Residue
F	CYS60
F	CYS62
F	CYS82
F	CYS85

site_id	AE6
Number of Residues	16
Details	binding site for residue CDL G 101

Chain	Residue
C	ASN125
C	LEU127
C	LEU131
C	PEK308
G	SER27
G	CYS31
G	ASN34
G	LEU37
G	HIS38
G	HOH203
a	PHE282
a	ASP300
a	TYR304
a	SER307
b	LEU78
b	TYR85

site_id	AE7
Number of Residues	5
Details	binding site for residue PEK G 102

Chain	Residue
G	ALA3
G	TPO11
G	HOH212
c	ARG80
c	GLU236

site_id	AE8
Number of Residues	7
Details	binding site for residue PGV G 103

Chain	Residue
C	TRP258
G	ALA1
c	TRP99
c	HIS103
c	LEU106
c	CHD302
c	HOH439

site_id	AE9
Number of Residues	3
Details	binding site for residue CHD J 101

Chain	Residue
J	ARG33
J	THR37
J	LEU40

site_id	AF1
Number of Residues	10
Details	binding site for residue TGL L 101

Chain	Residue
A	LEU21
A	TRP25
A	PHE400
A	ILE472
L	ILE11
L	PRO12
L	PHE13
L	ARG20
L	MET25
L	PHE29

site_id	AF2
Number of Residues	7
Details	binding site for residue DMU M 101

Chain	Residue
A	PHE459
D	TRP98
M	LEU28
M	GLY31
M	TRP32
M	TYR35
M	HIS36

site_id	AF3
Number of Residues	22
Details	binding site for residue HEA a 601

Chain	Residue
a	MET28
a	THR31
a	SER34
a	ARG38
a	TYR54
a	VAL58
a	HIS61
a	ALA62
a	MET65
a	VAL70
a	GLY125
a	TRP126
a	TYR371
a	PHE377
a	HIS378
a	PHE425
a	GLN428
a	ARG438
a	ARG439
a	VAL465
a	HOH722
a	HOH725

site_id	AF4
Number of Residues	27
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	HIS376
a	PHE377
a	VAL380
a	LEU381
a	ARG438
a	CMO608
a	HOH721
a	HOH748
a	HOH780
a	HOH788

site_id	AF5
Number of Residues	4
Details	binding site for residue CU a 603

Chain	Residue
a	HIS240
a	HIS290
a	HIS291
a	CMO608

site_id	AF6
Number of Residues	5
Details	binding site for residue MG a 604

Chain	Residue
a	HIS368
a	ASP369
b	GLU198
b	HOH429
b	HOH435

site_id	AF7
Number of Residues	4
Details	binding site for residue NA a 605

Chain	Residue
a	GLU40
a	GLY45
a	SER441
a	ASP442

site_id	AF8
Number of Residues	5
Details	binding site for residue TGL a 606

Chain	Residue
a	TRP334
b	HOH461
d	THR75
d	TRP78
d	VAL81

site_id	AF9
Number of Residues	10
Details	binding site for residue PGV a 607

Chain	Residue
a	ASN406
a	THR408
a	TRP409
a	HOH705
d	ALA84
k	PHE9
k	HIS10
m	ALA3
m	LYS4
m	GLN15

site_id	AG1
Number of Residues	4
Details	binding site for residue CMO a 608

Chain	Residue
a	HIS240
a	VAL243
a	HEA602
a	CU603

site_id	AG2
Number of Residues	11
Details	binding site for residue CHD b 301

Chain	Residue
C	PEK308
G	ARG14
G	ARG17
G	PHE18
G	GLY22
a	MET271
b	GLN59
b	GLU62
b	THR63
b	HOH431
b	HOH440

site_id	AG3
Number of Residues	6
Details	binding site for residue CUA b 302

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

site_id	AG4
Number of Residues	14
Details	binding site for residue PGV c 301

Chain	Residue
a	PHE94
a	PRO95
a	ARG96
a	MET97
a	HOH709
c	HIS9
c	ASN50
c	MET54
c	TRP57
c	TRP58
c	GLU64
c	HIS71
c	PHE93
g	PEK102

site_id	AG5
Number of Residues	8
Details	binding site for residue CHD c 302

Chain	Residue
G	PGV103
a	HIS233
a	ASP300
a	THR301
a	TYR304
c	TRP99
c	HIS103
c	HOH439

site_id	AG6
Number of Residues	7
Details	binding site for residue PEK c 303

Chain	Residue
A	TRP275
B	GLN59
B	THR66
c	HIS158
c	GLN161
g	ARG17
g	CDL103

site_id	AG7
Number of Residues	17
Details	binding site for residue PGV c 304

Chain	Residue
c	TRP58
c	VAL61
c	SER65
c	THR66
c	THR213
c	PHE214
c	ARG221
c	HIS226
c	PHE227
c	THR228
c	HIS231
c	HIS232
c	PHE233
c	GLY234
c	CDL305
c	HOH432
f	HOH201

site_id	AG8
Number of Residues	12
Details	binding site for residue CDL c 305

Chain	Residue
c	TYR55
c	ARG59
c	ILE62
c	ARG63
c	PHE67
c	VAL217
c	PHE220
c	LYS224
c	HIS226
c	PGV304
j	LYS8
j	THR27

site_id	AG9
Number of Residues	3
Details	binding site for residue CHD c 306

Chain	Residue
c	ARG156
c	PHE164
j	PHE1

site_id	AH1
Number of Residues	8
Details	binding site for residue DMU m 401

Chain	Residue
a	LEU35
d	TRP98
d	TYR102
m	LEU27
m	LEU28
m	TRP32
m	TYR35
m	HIS36

site_id	AH2
Number of Residues	5
Details	binding site for residue PSC e 201

Chain	Residue
b	HIS52
b	VAL61
e	HIS5
e	GLU6
e	ASP8

site_id	AH3
Number of Residues	4
Details	binding site for residue ZN f 101

Chain	Residue
f	CYS60
f	CYS62
f	CYS82
f	CYS85

site_id	AH4
Number of Residues	3
Details	binding site for residue DMU c 307

Chain	Residue
c	MET40
g	GLY63
g	HOH202

site_id	AH5
Number of Residues	15
Details	binding site for residue PEK g 102

Chain	Residue
a	THR207
c	TYR181
c	TYR182
c	ALA184
c	PHE186
c	THR187
c	ILE188
c	PHE198
c	LEU206
c	PGV301
g	THR68
g	PHE69
g	PHE70
g	HIS71
g	ASN76

site_id	AH6
Number of Residues	18
Details	binding site for residue CDL g 103

Chain	Residue
A	ASP300
A	SER307
A	ILE311
B	LEU78
B	LEU81
C	CHD301
c	LEU131
c	PEK303
g	ALA1
g	SER27
g	CYS31
g	ASN34
g	HIS38
g	HOH201
g	HOH208
g	HOH210
g	HOH214
g	HOH215

site_id	AH7
Number of Residues	5
Details	binding site for residue TGL i 101

Chain	Residue
a	ASN422
a	LEU433
b	LEU7
b	LEU28
i	ARG43

site_id	AH8
Number of Residues	4
Details	binding site for residue CHD j 101

Chain	Residue
j	TYR32
j	ARG33
j	MET36
j	THR37

site_id	AH9
Number of Residues	8
Details	binding site for residue TGL l 101

Chain	Residue
a	PHE2
a	LEU18
a	PHE400
l	ILE11
l	PHE13
l	MET24
l	PHE28
l	PHE29

site_id	AI1
Number of Residues	18
Details	binding site for Di-peptide HIS a 240 and TYR a 244

Chain	Residue
a	TRP236
a	PHE238
a	GLY239
a	PRO241
a	GLU242
a	VAL243
a	ILE245
a	LEU246
a	ILE247
a	LEU248
a	ILE280
a	GLY284
a	VAL287
a	HIS290
a	ILE312
a	HEA602
a	CU603
a	CMO608

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)