Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6J8M

Low-dose structure of bovine heart cytochrome c oxidase in the fully oxidized state determined using 30 keV X-ray

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	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	0022900	biological_process	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	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	0045277	cellular_component	respiratory chain complex IV
I	0005743	cellular_component	mitochondrial inner membrane
I	0006119	biological_process	oxidative phosphorylation
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	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	0022900	biological_process	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	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	0045277	cellular_component	respiratory chain complex IV
V	0005743	cellular_component	mitochondrial inner membrane
V	0006119	biological_process	oxidative phosphorylation
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	31
Details	binding site for residue HEA A 601

Chain	Residue
A	GLY27
A	ALA62
A	MET65
A	VAL70
A	ILE73
A	GLY125
A	TRP126
A	TYR371
A	PHE377
A	HIS378
A	SER382
A	MET28
A	PHE393
A	MET417
A	PHE425
A	GLN428
A	ARG438
A	ARG439
A	SER458
A	VAL465
A	MET468
A	HOH724
A	THR31
A	HOH725
A	HOH840
A	SER34
A	ILE37
A	ARG38
A	TYR54
A	VAL58
A	HIS61

site_id	AC2
Number of Residues	29
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	PER607
A	HOH715
A	HOH733
A	HOH793
A	HOH811
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	PER607

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

Chain	Residue
A	HIS368
A	ASP369
B	GLU198
B	HOH428
B	HOH447
B	HOH543

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

Chain	Residue
A	GLU40
A	GLY45
A	SER441
A	HOH827

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

Chain	Residue
A	ASN406
A	THR408
A	TRP409
A	HOH702
A	HOH922
D	ALA84
D	PHE87
K	PHE9
K	HIS10
M	PRO12
M	GLN15
M	ALA16
M	LEU19
M	SER20

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

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

site_id	AC8
Number of Residues	16
Details	binding site for residue PGV A 608

Chain	Residue
C	ASN50
C	MET54
C	TRP57
C	TRP58
C	GLU64
C	HIS71
C	LEU79
C	GLU90
C	PEK302
C	HOH419
A	PHE94
A	PRO95
A	ARG96
A	MET97
A	HOH755
C	HIS9

site_id	AC9
Number of Residues	10
Details	binding site for residue TGL B 301

Chain	Residue
A	TYR379
A	ASN422
A	PHE426
A	PHE430
A	LEU433
B	LEU7
B	LEU28
B	PHE32
B	SER35
I	ARG43

site_id	AD1
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	AD2
Number of Residues	12
Details	binding site for residue CHD B 303

Chain	Residue
A	MET271
B	GLN59
B	GLU62
B	THR63
B	THR66
B	HOH432
B	HOH443
P	PEK302
T	ARG14
T	ARG17
T	PHE21
T	GLY22

site_id	AD3
Number of Residues	5
Details	binding site for residue NA C 301

Chain	Residue
C	HIS148
C	MET152
C	HIS232
C	GLU236
C	HOH529

site_id	AD4
Number of Residues	21
Details	binding site for residue PEK C 302

Chain	Residue
A	VAL155
A	ALA203
A	PGV608
A	HOH898
C	TRP34
C	TYR181
C	TYR182
C	ALA184
C	PHE186
C	THR187
C	ILE188
C	PHE198
C	GLY202
C	PHE203
G	TRP62
G	THR68
G	PHE69
G	PHE70
G	HIS71
G	ASN76
G	HOH227

site_id	AD5
Number of Residues	12
Details	binding site for residue PEK C 303

Chain	Residue
C	LYS157
C	HIS158
C	GLN161
C	PHE164
C	THR168
C	TYR172
C	HOH426
C	HOH503
F	ALA1
G	ARG17
G	CDL101
O	CHD301

site_id	AD6
Number of Residues	18
Details	binding site for residue PGV C 304

Chain	Residue
C	TRP58
C	VAL61
C	SER65
C	THR66
C	ILE210
C	PHE214
C	ARG221
C	HIS226
C	PHE227
C	HIS231
C	HIS232
C	PHE233
C	GLY234
C	CDL306
C	HOH410
C	HOH438
C	HOH469
F	HOH224

site_id	AD7
Number of Residues	9
Details	binding site for residue PGV C 305

Chain	Residue
B	HOH527
C	TRP99
C	TYR102
C	HIS103
C	ALA107
C	HOH437
C	HOH511
H	ASN24
T	CDL103

site_id	AD8
Number of Residues	19
Details	binding site for residue CDL C 306

Chain	Residue
C	MET51
C	LEU52
C	MET54
C	TYR55
C	ARG59
C	ILE62
C	ARG63
C	PHE67
C	THR213
C	PHE220
C	ARG221
C	LYS224
C	HIS226
C	PGV304
C	HOH428
C	HOH446
C	HOH453
C	HOH541
J	LYS8

site_id	AD9
Number of Residues	7
Details	binding site for residue CHD C 307

Chain	Residue
C	ARG156
C	GLN161
C	PHE164
C	LEU223
C	HOH411
C	HOH456
J	PHE1

site_id	AE1
Number of Residues	10
Details	binding site for residue CHD C 308

Chain	Residue
A	HIS233
A	ASP300
A	THR301
A	TYR304
C	TRP99
C	HIS103
C	HOH429
C	HOH482
P	LEU127
T	CDL103

site_id	AE2
Number of Residues	6
Details	binding site for residue DMU C 309

Chain	Residue
C	MET33
C	PHE37
J	SER46
J	TYR48
J	CYS49
J	TRP52

site_id	AE3
Number of Residues	18
Details	binding site for residue TGL D 201

Chain	Residue
A	TRP334
A	LEU342
A	GLY343
A	PHE418
A	VAL419
A	HOH701
A	HOH970
B	ILE42
B	THR47
B	HOH554
D	ARG73
D	THR75
D	GLU77
D	TRP78
D	HOH356
D	HOH392
I	ARG16
I	HIS20

site_id	AE4
Number of Residues	11
Details	binding site for residue PSC E 201

Chain	Residue
A	PHE321
A	HIS328
B	HIS52
B	MET56
B	TRP65
B	HOH596
E	ASP8
E	PHE11
E	LEU41
E	HOH374
I	ARG10

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	21
Details	binding site for residue CDL G 101

Chain	Residue
C	LEU127
C	LEU131
C	PEK303
G	SER27
G	LEU30
G	CYS31
G	ASN34
G	LEU37
G	HIS38
G	PEK102
G	HOH216
N	PHE282
N	TYR304
N	SER307
N	ILE311
O	ALA77
O	LEU78
O	LEU81
O	ARG82
O	TYR85
P	PGV304

site_id	AE7
Number of Residues	13
Details	binding site for residue PEK G 102

Chain	Residue
G	SER2
G	ALA3
G	LYS5
G	GLY6
G	HIS8
G	CDL101
P	ARG80
P	ILE84
P	THR95
P	PHE98
P	TRP240
P	VAL247
P	HOH431

site_id	AE8
Number of Residues	5
Details	binding site for residue CHD J 101

Chain	Residue
J	TYR32
J	ARG33
J	MET36
J	THR37
J	LEU40

site_id	AE9
Number of Residues	18
Details	binding site for residue TGL L 101

Chain	Residue
A	PHE2
A	THR17
A	PHE22
A	TRP25
A	PRO106
A	PHE400
A	SER401
A	ILE472
L	ILE11
L	PRO12
L	PHE13
L	SER14
L	ARG20
L	MET24
L	PHE29
L	SER31
L	HOH223
L	HOH226

site_id	AF1
Number of Residues	8
Details	binding site for residue DMU M 101

Chain	Residue
D	TRP98
D	TYR102
D	HOH329
M	LEU28
M	GLY31
M	TRP32
M	TYR35
M	HIS36

site_id	AF2
Number of Residues	29
Details	binding site for residue HEA N 601

Chain	Residue
N	MET28
N	THR31
N	SER34
N	ILE37
N	ARG38
N	TYR54
N	VAL58
N	HIS61
N	ALA62
N	MET65
N	ILE66
N	VAL70
N	GLY125
N	TRP126
N	TYR371
N	PHE377
N	HIS378
N	SER382
N	VAL386
N	MET417
N	PHE425
N	GLN428
N	ARG438
N	ARG439
N	MET468
N	TGL611
N	HOH717
N	HOH770
N	HOH778

site_id	AF3
Number of Residues	30
Details	binding site for residue HEA N 602

Chain	Residue
N	TRP126
N	TRP236
N	VAL243
N	TYR244
N	HIS290
N	HIS291
N	THR309
N	ALA313
N	THR316
N	GLY317
N	GLY352
N	LEU353
N	GLY355
N	ILE356
N	LEU358
N	ALA359
N	ASP364
N	HIS368
N	VAL373
N	HIS376
N	PHE377
N	VAL380
N	LEU381
N	ARG438
N	PER607
N	HOH719
N	HOH721
N	HOH806
N	HOH815
O	ILE34

site_id	AF4
Number of Residues	4
Details	binding site for residue CU N 603

Chain	Residue
N	HIS240
N	HIS290
N	HIS291
N	PER607

site_id	AF5
Number of Residues	6
Details	binding site for residue MG N 604

Chain	Residue
N	HIS368
N	ASP369
O	GLU198
O	HOH410
O	HOH471
O	HOH512

site_id	AF6
Number of Residues	4
Details	binding site for residue NA N 605

Chain	Residue
N	GLU40
N	GLY45
N	SER441
N	HOH822

site_id	AF7
Number of Residues	10
Details	binding site for residue PGV N 606

Chain	Residue
N	ASN406
N	THR408
N	TRP409
N	HOH939
Q	ALA84
X	PHE9
X	HOH107
Z	PRO12
Z	GLN15
Z	LEU19

site_id	AF8
Number of Residues	5
Details	binding site for residue PER N 607

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

site_id	AF9
Number of Residues	13
Details	binding site for residue TGL N 608

Chain	Residue
N	PHE346
N	TYR379
N	ASN422
N	PHE426
N	HIS429
N	PHE430
N	LEU433
O	LEU7
O	GLY8
O	LEU28
O	PHE32
O	SER35
O	LEU39

site_id	AG1
Number of Residues	20
Details	binding site for residue PGV N 609

Chain	Residue
N	PHE94
N	PRO95
N	ARG96
N	MET97
N	LEU152
N	HOH703
N	HOH740
P	HIS9
P	GLY20
P	ALA24
P	ASN50
P	MET54
P	TRP57
P	TRP58
P	VAL61
P	GLU64
P	HIS71
P	LEU79
P	GLU90
T	PEK102

site_id	AG2
Number of Residues	10
Details	binding site for residue CHD N 610

Chain	Residue
C	LEU127
N	HIS233
N	ASP300
N	THR301
N	TYR304
N	HOH705
N	HOH792
N	HOH852
P	TRP99
P	HIS103

site_id	AG3
Number of Residues	18
Details	binding site for residue TGL N 611

Chain	Residue
N	PHE2
N	THR17
N	LEU18
N	LEU20
N	PHE22
N	LEU113
N	PHE400
N	HEA601
N	HOH930
Y	ASN10
Y	ILE11
Y	PRO12
Y	PHE13
Y	SER14
Y	ARG20
Y	MET24
Y	PHE28
Y	PHE29

site_id	AG4
Number of Residues	13
Details	binding site for residue CHD O 301

Chain	Residue
C	PEK303
G	ARG14
G	ARG17
G	PHE21
G	GLY22
G	HOH219
N	MET271
N	TRP275
O	GLN59
O	GLU62
O	THR63
O	HOH405
O	HOH415

site_id	AG5
Number of Residues	6
Details	binding site for residue CUA O 302

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

site_id	AG6
Number of Residues	3
Details	binding site for residue NA P 301

Chain	Residue
P	HIS148
P	HIS232
P	GLU236

site_id	AG7
Number of Residues	14
Details	binding site for residue PEK P 302

Chain	Residue
B	CHD303
B	HOH532
P	LYS157
P	HIS158
P	THR168
P	TYR172
P	HOH496
S	ALA1
T	ARG17
T	PHE21
T	GLY22
T	TRP36
T	CDL103
T	HOH208

site_id	AG8
Number of Residues	19
Details	binding site for residue PGV P 303

Chain	Residue
P	TRP58
P	VAL61
P	SER65
P	THR66
P	ILE210
P	PHE214
P	ARG221
P	HIS226
P	PHE227
P	THR228
P	HIS231
P	HIS232
P	PHE233
P	GLY234
P	CDL305
P	HOH419
P	HOH448
P	HOH484
S	HOH230

site_id	AG9
Number of Residues	12
Details	binding site for residue PGV P 304

Chain	Residue
G	ALA1
G	CDL101
O	HOH484
P	THR95
P	TRP99
P	TYR102
P	HIS103
P	ALA107
P	HOH407
P	HOH474
P	HOH488
U	ASN24

site_id	AH1
Number of Residues	19
Details	binding site for residue CDL P 305

Chain	Residue
P	MET51
P	TYR55
P	ARG59
P	ILE62
P	ARG63
P	PHE67
P	VAL217
P	PHE220
P	LYS224
P	HIS226
P	PGV303
P	HOH457
P	HOH477
P	HOH485
P	HOH492
P	HOH503
P	HOH529
P	HOH537
W	LYS8

site_id	AH2
Number of Residues	8
Details	binding site for residue CHD P 306

Chain	Residue
P	ARG156
P	PHE164
P	LEU223
P	HOH426
P	HOH449
P	HOH476
P	HOH493
W	PHE1

site_id	AH3
Number of Residues	7
Details	binding site for residue DMU P 307

Chain	Residue
N	LEU110
P	MET33
P	PHE37
W	SER46
W	TYR48
W	CYS49
W	TRP52

site_id	AH4
Number of Residues	11
Details	binding site for residue TGL Q 201

Chain	Residue
N	TRP334
N	PHE414
N	HOH708
N	HOH966
O	ILE42
O	THR47
Q	THR75
Q	GLU77
Q	TRP78
V	ARG16
V	HIS20

site_id	AH5
Number of Residues	13
Details	binding site for residue PSC R 201

Chain	Residue
N	PHE321
N	HIS328
O	ILE41
O	MET56
O	ASP57
O	TRP65
R	HIS5
R	GLU6
R	THR7
R	ASP8
R	HOH335
R	HOH382
V	ARG10

site_id	AH6
Number of Residues	4
Details	binding site for residue ZN S 101

Chain	Residue
S	CYS60
S	CYS62
S	CYS82
S	CYS85

site_id	AH7
Number of Residues	10
Details	binding site for residue PEK T 101

Chain	Residue
C	TYR81
C	VAL91
C	THR95
C	TRP240
C	VAL247
T	SER2
T	ALA3
T	LYS5
T	HIS8
T	CDL103

site_id	AH8
Number of Residues	19
Details	binding site for residue PEK T 102

Chain	Residue
N	HIS151
N	VAL155
N	ALA203
N	PGV609
P	TYR181
P	TYR182
P	ALA184
P	PHE186
P	THR187
P	ILE188
P	PHE198
T	TRP62
T	THR68
T	PHE69
T	PHE70
T	HIS71
T	ASN76
T	HOH202
T	HOH225

site_id	AH9
Number of Residues	26
Details	binding site for residue CDL T 103

Chain	Residue
A	PHE282
A	ASP300
A	TYR304
A	ALA308
A	ILE311
B	ALA77
B	LEU78
B	LEU81
B	TYR85
B	HOH525
C	PGV305
C	CHD308
P	ASN125
P	LEU127
P	GLU128
P	LEU131
P	TRP258
P	PEK302
T	SER27
T	LEU30
T	CYS31
T	ASN34
T	LEU37
T	HIS38
T	PEK101
T	HOH239

site_id	AI1
Number of Residues	7
Details	binding site for residue CHD W 101

Chain	Residue
N	ILE3
W	TYR32
W	ARG33
W	MET36
W	THR37
W	LEU40
W	HOH219

site_id	AI2
Number of Residues	10
Details	binding site for residue DMU Z 101

Chain	Residue
Q	TRP98
Q	TYR102
Z	LEU27
Z	LEU28
Z	GLY31
Z	TRP32
Z	LEU34
Z	TYR35
Z	HIS36
Z	HOH202

site_id	AI3
Number of Residues	16
Details	binding site for Di-peptide HIS N 240 and TYR N 244

Chain	Residue
N	TRP236
N	PHE238
N	GLY239
N	PRO241
N	GLU242
N	VAL243
N	ILE245
N	LEU246
N	ILE247
N	LEU248
N	ILE280
N	GLY284
N	HIS290
N	HEA602
N	CU603
N	PER607

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)