Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5X1B

CO bound cytochrome c oxidase at 20 nsec after pump laser irradiation to release CO from O2 reduction center

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
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
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
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
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
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
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
N	0004129	molecular_function	cytochrome-c oxidase activity
N	0005743	cellular_component	mitochondrial inner membrane
N	0006119	biological_process	oxidative phosphorylation
N	0009060	biological_process	aerobic respiration
N	0016020	cellular_component	membrane
N	0020037	molecular_function	heme binding
N	0022904	biological_process	respiratory electron transport chain
N	0045277	cellular_component	respiratory chain complex IV
N	0046872	molecular_function	metal ion binding
N	1902600	biological_process	proton transmembrane transport
O	0004129	molecular_function	cytochrome-c oxidase activity
O	0005507	molecular_function	copper ion binding
O	0005739	cellular_component	mitochondrion
O	0005743	cellular_component	mitochondrial inner membrane
O	0016020	cellular_component	membrane
O	0016491	molecular_function	oxidoreductase activity
O	0017004	biological_process	cytochrome complex assembly
O	0022900	biological_process	electron transport chain
O	0022904	biological_process	respiratory electron transport chain
O	0031966	cellular_component	mitochondrial membrane
O	0042773	biological_process	ATP synthesis coupled electron transport
O	0045277	cellular_component	respiratory chain complex IV
O	0046872	molecular_function	metal ion binding
O	1902600	biological_process	proton transmembrane transport
P	0004129	molecular_function	cytochrome-c oxidase activity
P	0005739	cellular_component	mitochondrion
P	0005743	cellular_component	mitochondrial inner membrane
P	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
P	0008535	biological_process	respiratory chain complex IV assembly
P	0009055	molecular_function	electron transfer activity
P	0016020	cellular_component	membrane
P	0019646	biological_process	aerobic electron transport chain
P	0022904	biological_process	respiratory electron transport chain
P	0045277	cellular_component	respiratory chain complex IV
P	1902600	biological_process	proton transmembrane transport
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
R	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
R	0045277	cellular_component	respiratory chain complex IV
S	0005740	cellular_component	mitochondrial envelope
S	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
S	0045277	cellular_component	respiratory chain complex IV
T	0005743	cellular_component	mitochondrial inner membrane
U	0005739	cellular_component	mitochondrion
U	0005743	cellular_component	mitochondrial inner membrane
U	0006119	biological_process	oxidative phosphorylation
U	0016020	cellular_component	membrane
U	0045277	cellular_component	respiratory chain complex IV
V	0005743	cellular_component	mitochondrial inner membrane
V	0006119	biological_process	oxidative phosphorylation
V	0016020	cellular_component	membrane
V	0045277	cellular_component	respiratory chain complex IV
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
Y	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
Y	0045277	cellular_component	respiratory chain complex IV
Z	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
Z	0045277	cellular_component	respiratory chain complex IV

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	binding site for residue HEA A 601

Chain	Residue
A	THR31
A	GLY125
A	TRP126
A	TYR371
A	PHE377
A	HIS378
A	PHE393
A	PHE425
A	GLN428
A	ARG438
A	ARG439
A	SER34
A	TYR440
A	MET468
A	HOH703
A	HOH743
A	HOH754
A	HOH755
A	ILE37
A	ARG38
A	TYR54
A	HIS61
A	ALA62
A	MET65
A	VAL70

site_id	AC2
Number of Residues	25
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	LEU358
A	ALA359
A	ASP364
A	HIS368
A	HIS376
A	PHE377
A	VAL380
A	ARG438
A	CMO606
A	HOH708
A	HOH729
A	HOH769
A	HOH783
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	CMO606

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

Chain	Residue
A	HIS368
A	ASP369
B	GLU198
B	HOH402
B	HOH425
B	HOH427

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

Chain	Residue
A	GLU40
A	GLY45
A	SER441
A	HOH793

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

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

site_id	AC7
Number of Residues	5
Details	binding site for residue TGL A 607

Chain	Residue
A	PHE426
A	PHE430
A	LEU433
B	LEU28
B	SER35

site_id	AC8
Number of Residues	12
Details	binding site for residue PGV A 608

Chain	Residue
A	PHE94
A	PRO95
A	ARG96
A	MET97
C	HIS9
C	ASN50
C	TRP57
C	TRP58
C	GLU64
C	HIS71
C	HOH403
C	HOH413

site_id	AC9
Number of Residues	3
Details	binding site for residue PGV A 609

Chain	Residue
A	ASN406
A	THR408
M	GLN15

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO A 610

Chain	Residue
A	TYR260
A	TYR261
A	VAL394
A	HIS395

site_id	AD2
Number of Residues	2
Details	binding site for residue EDO A 611

Chain	Residue
C	PGV308
T	CDL103

site_id	AD3
Number of Residues	8
Details	binding site for residue EDO A 612

Chain	Residue
A	THR10
A	ASN11
A	TYR502
C	PRO13
L	TYR3
A	ASN4
A	ARG5
A	SER9

site_id	AD4
Number of Residues	4
Details	binding site for residue EDO A 613

Chain	Residue
A	GLN43
D	LYS100
D	HOH308
K	GLU39

site_id	AD5
Number of Residues	8
Details	binding site for residue EDO A 614

Chain	Residue
A	LEU35
A	ARG38
A	ALA39
A	SER455
A	SER458
A	PHE459
D	GLU99
D	TYR104

site_id	AD6
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	AD7
Number of Residues	8
Details	binding site for residue CHD B 302

Chain	Residue
A	MET271
B	GLU62
B	THR63
B	HOH452
T	ARG14
T	ARG17
T	PEK102
T	HOH206

site_id	AD8
Number of Residues	6
Details	binding site for residue PSC B 303

Chain	Residue
B	HIS52
B	ASP57
B	GLU60
E	GLU6
E	ASP8
I	ARG10

site_id	AD9
Number of Residues	6
Details	binding site for residue EDO B 304

Chain	Residue
A	TYR447
A	HOH796
B	ALA2
B	GLN10
B	PRO166
B	TYR193

site_id	AE1
Number of Residues	6
Details	binding site for residue EDO B 305

Chain	Residue
B	ALA12
B	THR13
B	SER14
B	GLU18
B	SER187
I	TYR51

site_id	AE2
Number of Residues	14
Details	binding site for residue PGV C 302

Chain	Residue
C	TRP58
C	VAL61
C	SER65
C	THR66
C	HIS207
C	ILE210
C	ARG221
C	HIS226
C	HIS231
C	PHE233
C	GLY234
C	HOH425
C	HOH451
F	HOH212

site_id	AE3
Number of Residues	8
Details	binding site for residue CDL C 303

Chain	Residue
C	TYR55
C	ARG63
C	PHE67
C	LEU175
C	PHE220
C	LYS224
C	HIS226
J	LYS8

site_id	AE4
Number of Residues	3
Details	binding site for residue CHD C 304

Chain	Residue
C	ARG156
C	PHE164
J	PHE1

site_id	AE5
Number of Residues	8
Details	binding site for residue CHD C 305

Chain	Residue
A	HIS233
A	ASP300
A	THR301
A	TYR304
C	TRP99
C	HIS103
C	PGV308
T	CDL103

site_id	AE6
Number of Residues	9
Details	binding site for residue PEK C 306

Chain	Residue
C	LYS157
C	HIS158
C	HOH412
C	HOH433
F	ALA1
G	ARG17
G	TRP36
O	GLN59
O	CHD302

site_id	AE7
Number of Residues	17
Details	binding site for residue CDL C 307

Chain	Residue
C	ASN125
C	LEU127
C	LEU131
C	HOH405
G	SER27
G	ASN34
G	HIS38
G	PEK102
G	PGV103
N	PHE282
N	ASP300
N	TYR304
N	SER307
O	ALA77
O	LEU78
O	LEU81
O	TYR85

site_id	AE8
Number of Residues	9
Details	binding site for residue PGV C 308

Chain	Residue
A	EDO611
C	TRP99
C	TYR102
C	HIS103
C	ALA107
C	CHD305
C	EDO309
H	ASN22
T	HOH213

site_id	AE9
Number of Residues	2
Details	binding site for residue EDO C 309

Chain	Residue
C	PGV308
C	HOH407

site_id	AF1
Number of Residues	1
Details	binding site for residue EDO C 310

Chain	Residue
C	HIS149

site_id	AF2
Number of Residues	1
Details	binding site for residue EDO C 311

Chain	Residue
C	THR145

site_id	AF3
Number of Residues	7
Details	binding site for residue TGL D 201

Chain	Residue
A	TRP334
B	THR47
D	THR75
D	GLU77
D	TRP78
I	ARG16
I	HIS20

site_id	AF4
Number of Residues	4
Details	binding site for residue ZN F 101

Chain	Residue
F	CYS60
F	CYS62
F	CYS82
F	CYS85

site_id	AF5
Number of Residues	4
Details	binding site for residue EDO F 102

Chain	Residue
A	TYR510
F	LYS37
F	ASN47
F	LEU48

site_id	AF6
Number of Residues	16
Details	binding site for residue PEK G 101

Chain	Residue
A	VAL155
C	TYR181
C	TYR182
C	ALA184
C	PHE186
C	THR187
C	ILE188
C	PHE198
C	GLY202
C	PHE203
G	THR68
G	PHE69
G	PHE70
G	HIS71
G	ASN76
G	HOH213

site_id	AF7
Number of Residues	9
Details	binding site for residue PEK G 102

Chain	Residue
C	CDL307
G	SER2
G	ALA3
G	HIS8
P	PHE98
P	TRP240
P	PHE244
P	VAL247
P	PHE251

site_id	AF8
Number of Residues	10
Details	binding site for residue PGV G 103

Chain	Residue
C	CDL307
G	ALA1
G	SER2
G	HOH202
G	HOH203
G	HOH215
P	TYR102
P	HIS103
P	ALA107
U	ASN22

site_id	AF9
Number of Residues	5
Details	binding site for residue EDO G 104

Chain	Residue
C	GLY120
G	ALA46
G	PHE47
G	ILE48
G	ARG54

site_id	AG1
Number of Residues	4
Details	binding site for residue CHD J 101

Chain	Residue
J	TYR32
J	ARG33
J	THR37
J	LEU40

site_id	AG2
Number of Residues	1
Details	binding site for residue EDO K 102

Chain	Residue
K	ALA33

site_id	AG3
Number of Residues	13
Details	binding site for residue TGL L 101

Chain	Residue
A	LEU21
A	TRP25
A	PHE400
A	HOH825
L	ASN10
L	ILE11
L	PRO12
L	PHE13
L	SER14
L	ARG20
L	PHE28
L	EDO102
L	HOH207

site_id	AG4
Number of Residues	1
Details	binding site for residue EDO L 102

Chain	Residue
L	TGL101

site_id	AG5
Number of Residues	5
Details	binding site for residue DMU M 101

Chain	Residue
D	TRP98
M	LEU28
M	GLY31
M	TRP32
M	TYR35

site_id	AG6
Number of Residues	23
Details	binding site for residue HEA N 601

Chain	Residue
N	THR31
N	SER34
N	ILE37
N	ARG38
N	TYR54
N	VAL58
N	HIS61
N	ALA62
N	MET65
N	VAL70
N	GLY125
N	TRP126
N	TYR371
N	PHE377
N	HIS378
N	SER382
N	PHE425
N	GLN428
N	ARG438
N	ARG439
N	MET468
N	HOH711
N	HOH729

site_id	AG7
Number of Residues	24
Details	binding site for residue HEA N 602

Chain	Residue
N	TRP126
N	TRP236
N	VAL243
N	TYR244
N	HIS290
N	THR309
N	ILE312
N	GLY317
N	GLY352
N	GLY355
N	LEU358
N	ALA359
N	ASP364
N	HIS368
N	HIS376
N	PHE377
N	VAL380
N	ARG438
N	CMO606
N	HOH715
N	HOH727
N	HOH745
N	HOH747
N	HOH798

site_id	AG8
Number of Residues	4
Details	binding site for residue CU N 603

Chain	Residue
N	HIS240
N	HIS290
N	HIS291
N	CMO606

site_id	AG9
Number of Residues	6
Details	binding site for residue MG N 604

Chain	Residue
N	HIS368
N	ASP369
N	HOH763
O	GLU198
O	HOH425
O	HOH450

site_id	AH1
Number of Residues	7
Details	binding site for residue NA N 605

Chain	Residue
N	GLU40
N	GLN43
N	GLY45
N	SER441
N	ASP442
N	HOH714
N	HOH774

site_id	AH2
Number of Residues	5
Details	binding site for residue CMO N 606

Chain	Residue
N	HIS240
N	VAL243
N	HIS291
N	HEA602
N	CU603

site_id	AH3
Number of Residues	5
Details	binding site for residue PGV N 607

Chain	Residue
N	ASN406
N	TRP409
Z	PRO12
Z	GLN15
Z	ALA16

site_id	AH4
Number of Residues	11
Details	binding site for residue PGV N 608

Chain	Residue
N	PHE94
N	PRO95
N	ARG96
N	MET97
P	HIS9
P	MET27
P	ASN50
P	TRP57
P	TRP58
P	GLU64
P	HIS71

site_id	AH5
Number of Residues	7
Details	binding site for residue TGL N 609

Chain	Residue
N	ASN422
N	PHE426
N	LEU433
N	HOH701
N	HOH815
O	LEU7
O	GLY8

site_id	AH6
Number of Residues	9
Details	binding site for residue TGL N 610

Chain	Residue
N	TRP334
N	LYS411
O	LEU39
O	THR47
Q	SER74
Q	GLU77
Q	MET86
Q	HOH214
V	ARG16

site_id	AH7
Number of Residues	9
Details	binding site for residue TGL N 611

Chain	Residue
N	THR17
N	TRP25
N	PHE400
N	PHE476
Y	PRO12
Y	PHE13
Y	SER14
Y	PHE28
Y	SER31

site_id	AH8
Number of Residues	5
Details	binding site for residue EDO N 612

Chain	Residue
N	TYR260
N	TYR261
N	HIS395
N	HOH731
Z	ILE1

site_id	AH9
Number of Residues	6
Details	binding site for residue CUA O 301

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

site_id	AI1
Number of Residues	11
Details	binding site for residue CHD O 302

Chain	Residue
C	PEK306
G	ARG14
G	ARG17
G	PHE21
G	GLY22
N	MET271
N	TRP275
O	GLN59
O	GLU62
O	THR63
O	HOH433

site_id	AI2
Number of Residues	17
Details	binding site for residue PEK P 302

Chain	Residue
N	HIS151
P	TYR181
P	TYR182
P	ALA184
P	PHE186
P	THR187
P	ILE188
P	PHE198
P	GLY202
P	PGV303
P	CDL304
P	HOH404
T	THR68
T	PHE69
T	PHE70
T	HIS71
T	ASN76

site_id	AI3
Number of Residues	19
Details	binding site for residue PGV P 303

Chain	Residue
P	TRP58
P	VAL61
P	SER65
P	THR66
P	PHE86
P	HIS207
P	ILE210
P	PHE214
P	ARG221
P	HIS226
P	PHE227
P	HIS231
P	HIS232
P	PHE233
P	GLY234
P	PEK302
P	CDL304
P	HOH428
P	HOH434

site_id	AI4
Number of Residues	9
Details	binding site for residue CDL P 304

Chain	Residue
P	MET51
P	TYR55
P	ARG63
P	PHE67
P	LYS224
P	HIS226
P	PEK302
P	PGV303
W	LYS8

site_id	AI5
Number of Residues	3
Details	binding site for residue CHD P 305

Chain	Residue
P	ARG156
P	PHE219
W	PHE1

site_id	AI6
Number of Residues	6
Details	binding site for residue CHD P 306

Chain	Residue
N	HIS233
N	THR301
N	TYR304
P	TRP99
P	HIS103
P	HOH435

site_id	AI7
Number of Residues	5
Details	binding site for residue PSC R 201

Chain	Residue
O	THR55
O	ASP57
O	TRP65
R	ASP40
R	LEU41

site_id	AI8
Number of Residues	4
Details	binding site for residue ZN S 101

Chain	Residue
S	CYS60
S	CYS62
S	CYS82
S	CYS85

site_id	AI9
Number of Residues	5
Details	binding site for residue PEK T 101

Chain	Residue
C	ARG80
T	SER2
T	ALA3
T	HIS8
T	HOH218

site_id	AJ1
Number of Residues	6
Details	binding site for residue PEK T 102

Chain	Residue
B	GLN59
B	CHD302
P	LYS157
P	HIS158
T	ARG17
T	CDL103

site_id	AJ2
Number of Residues	20
Details	binding site for residue CDL T 103

Chain	Residue
A	PHE282
A	ASP300
A	SER307
A	EDO611
A	HOH812
B	LEU78
B	LEU81
B	TYR85
B	GLU89
C	CHD305
P	ASN125
P	LEU131
P	TRP258
T	CYS31
T	ASN34
T	LEU37
T	HIS38
T	PEK102
T	HOH205
T	HOH210

site_id	AJ3
Number of Residues	5
Details	binding site for residue EDO T 104

Chain	Residue
A	MET278
T	LYS5
T	PHE18
T	LEU19
T	LEU23

site_id	AJ4
Number of Residues	5
Details	binding site for residue CHD W 101

Chain	Residue
W	TYR32
W	ARG33
W	MET36
W	THR37
W	LEU40

site_id	AJ5
Number of Residues	6
Details	binding site for residue DMU Z 101

Chain	Residue
Q	TRP98
Z	LEU27
Z	LEU28
Z	GLY31
Z	TRP32
Z	TYR35

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

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