Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5B1A

Bovine heart cytochrome c oxidase in the fully oxidized state at 1.5 angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004129	molecular_function	cytochrome-c oxidase activity
A	0005739	cellular_component	mitochondrion
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	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	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	0005739	cellular_component	mitochondrion
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	0005739	cellular_component	mitochondrion
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	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	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	0005739	cellular_component	mitochondrion
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	28
Details	binding site for residue HEA A 601

Chain	Residue
A	MET28
A	MET65
A	VAL70
A	GLY125
A	TRP126
A	TYR371
A	PHE377
A	HIS378
A	SER382
A	PHE393
A	MET417
A	THR31
A	PHE425
A	GLN428
A	ARG438
A	ARG439
A	SER458
A	MET468
A	HOH729
A	HOH731
A	HOH784
A	SER34
A	ILE37
A	ARG38
A	TYR54
A	VAL58
A	HIS61
A	ALA62

site_id	AC2
Number of Residues	30
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	LEU353
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	PER606
A	HOH721
A	HOH741
A	HOH817
A	HOH831
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	PER606

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

Chain	Residue
A	HIS368
A	ASP369
B	GLU198
B	HOH447
B	HOH486
B	HOH521

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

Chain	Residue
A	GLU40
A	GLY45
A	SER441
A	HOH877

site_id	AC6
Number of Residues	5
Details	binding site for residue PER A 606

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

site_id	AC7
Number of Residues	16
Details	binding site for residue PGV A 607

Chain	Residue
A	PHE94
A	PRO95
A	ARG96
A	MET97
A	HOH767
C	HIS9
C	GLY20
C	ASN50
C	MET54
C	TRP57
C	TRP58
C	GLU64
C	HIS71
C	GLY82
C	HOH489
G	PEK101

site_id	AC8
Number of Residues	14
Details	binding site for residue PGV A 608

Chain	Residue
A	HOH886
A	HOH930
D	PHE87
K	HIS10
M	GLN15
M	LEU19
M	SER20
M	HOH225
A	ASN406
A	THR408
A	HOH702
A	HOH785
A	HOH830
A	HOH881

site_id	AC9
Number of Residues	11
Details	binding site for residue TGL B 301

Chain	Residue
A	ASN422
A	PHE430
A	LEU433
B	LEU7
B	LEU28
B	VAL31
B	PHE32
B	SER35
B	SER36
B	HOH589
I	HOH173

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
A	TRP275
B	GLN59
B	GLU62
B	THR63
B	HOH419
B	HOH444
B	HOH468
P	PEK308
T	ARG14
T	ARG17
T	GLY22

site_id	AD3
Number of Residues	15
Details	binding site for residue PSC B 304

Chain	Residue
A	PHE321
B	HIS52
B	THR55
B	MET56
B	ASP57
B	GLU60
B	HOH405
B	HOH538
E	GLU6
E	ASP8
E	PHE11
E	HOH275
E	HOH280
I	ARG10
I	LEU17

site_id	AD4
Number of Residues	22
Details	binding site for residue PGV C 302

Chain	Residue
C	MET51
C	MET54
C	TRP58
C	VAL61
C	SER65
C	THR66
C	HIS71
C	ILE210
C	PHE214
C	ARG221
C	HIS226
C	PHE227
C	THR228
C	HIS231
C	HIS232
C	PHE233
C	GLY234
C	CDL303
C	HOH426
C	HOH439
C	HOH446
C	HOH510

site_id	AD5
Number of Residues	18
Details	binding site for residue CDL C 303

Chain	Residue
C	THR48
C	MET51
C	TYR55
C	TRP58
C	ARG59
C	ILE62
C	ARG63
C	PHE67
C	THR174
C	THR213
C	VAL217
C	PHE220
C	LYS224
C	HIS226
C	PGV302
C	HOH412
J	LYS8
J	LEU31

site_id	AD6
Number of Residues	7
Details	binding site for residue CHD C 304

Chain	Residue
C	ARG156
C	GLN161
C	PHE164
C	PHE219
C	LEU223
C	HOH461
J	PHE1

site_id	AD7
Number of Residues	14
Details	binding site for residue CHD C 305

Chain	Residue
A	HIS233
A	ASP300
A	THR301
A	TYR304
A	HOH723
C	TRP99
C	HIS103
C	HOH415
C	HOH418
C	HOH432
C	HOH506
C	HOH508
C	HOH520
P	LEU127

site_id	AD8
Number of Residues	15
Details	binding site for residue PEK C 306

Chain	Residue
C	LYS157
C	HIS158
C	GLN161
C	TYR172
C	HOH425
C	HOH481
F	ALA1
G	ARG17
G	PHE21
G	GLY22
G	CDL102
N	SER279
N	ILE311
O	GLN59
O	CHD302

site_id	AD9
Number of Residues	11
Details	binding site for residue PGV C 307

Chain	Residue
A	HOH836
C	TRP99
C	TYR102
C	HIS103
C	ALA107
C	HOH460
C	HOH476
C	HOH514
C	HOH558
H	ASN24
H	HOH120

site_id	AE1
Number of Residues	16
Details	binding site for residue TGL D 201

Chain	Residue
A	TRP334
A	PHE414
A	PHE418
A	HOH964
B	ILE42
B	LYS49
B	HOH566
B	HOH576
D	ARG73
D	THR75
D	GLU77
D	TRP78
D	HOH419
D	HOH452
I	ARG16
I	HIS20

site_id	AE2
Number of Residues	4
Details	binding site for residue ZN F 101

Chain	Residue
F	CYS60
F	CYS62
F	CYS82
F	CYS85

site_id	AE3
Number of Residues	21
Details	binding site for residue PEK G 101

Chain	Residue
A	HIS151
A	VAL155
A	ILE158
A	PGV607
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	HOH239

site_id	AE4
Number of Residues	25
Details	binding site for residue CDL G 102

Chain	Residue
C	LEU127
C	LEU131
C	TYR253
C	VAL254
C	TRP258
C	PEK306
G	SER27
G	LEU30
G	CYS31
G	ASN34
G	LEU37
G	HIS38
G	PEK103
G	HOH205
G	HOH209
G	HOH258
G	HOH267
N	PHE282
N	ILE286
N	SER307
N	ILE311
O	ILE74
O	ALA77
O	LEU78
O	HOH488

site_id	AE5
Number of Residues	13
Details	binding site for residue PEK G 103

Chain	Residue
G	SER2
G	ALA3
G	LYS5
G	GLY6
G	HIS8
G	CDL102
P	LYS77
P	ARG80
P	TYR81
P	THR95
P	PHE98
P	TRP240
P	VAL247

site_id	AE6
Number of Residues	9
Details	binding site for residue DMU J 101

Chain	Residue
C	LEU25
C	MET33
C	PHE37
J	SER46
J	TYR48
J	CYS49
J	LEU50
J	TRP52
J	HOH204

site_id	AE7
Number of Residues	5
Details	binding site for residue CHD J 102

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

site_id	AE8
Number of Residues	14
Details	binding site for residue TGL L 101

Chain	Residue
A	THR17
A	LEU21
A	PHE22
A	TRP25
A	LEU113
A	PHE393
A	PHE400
L	ILE11
L	PRO12
L	PHE13
L	SER14
L	ARG20
L	PHE29
L	SER31

site_id	AE9
Number of Residues	8
Details	binding site for residue DMU M 101

Chain	Residue
D	TRP98
M	LEU27
M	LEU28
M	GLY31
M	TRP32
M	TYR35
M	HIS36
M	HOH210

site_id	AF1
Number of Residues	27
Details	binding site for residue HEA N 601

Chain	Residue
N	ALA24
N	MET28
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	VAL386
N	MET417
N	PHE425
N	GLN428
N	ARG438
N	ARG439
N	HOH718
N	HOH739
N	HOH776

site_id	AF2
Number of Residues	29
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	ILE312
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	PER606
N	HOH706
N	HOH747
N	HOH771
N	HOH787

site_id	AF3
Number of Residues	4
Details	binding site for residue CU N 603

Chain	Residue
N	HIS240
N	HIS290
N	HIS291
N	PER606

site_id	AF4
Number of Residues	6
Details	binding site for residue MG N 604

Chain	Residue
N	HIS368
N	ASP369
O	GLU198
O	HOH439
O	HOH479
O	HOH548

site_id	AF5
Number of Residues	4
Details	binding site for residue NA N 605

Chain	Residue
N	GLU40
N	GLY45
N	SER441
N	HOH835

site_id	AF6
Number of Residues	5
Details	binding site for residue PER N 606

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

site_id	AF7
Number of Residues	17
Details	binding site for residue PGV N 607

Chain	Residue
N	PHE94
N	PRO95
N	ARG96
N	MET97
N	HOH728
P	HIS9
P	GLY20
P	ASN50
P	MET54
P	TRP57
P	TRP58
P	GLU64
P	HIS71
P	GLY82
P	SER89
P	HOH486
T	PEK101

site_id	AF8
Number of Residues	10
Details	binding site for residue TGL N 608

Chain	Residue
N	ASN422
N	PHE426
N	PHE430
N	LEU433
N	HOH866
O	LEU7
O	LEU28
O	PHE32
O	SER35
V	ARG43

site_id	AF9
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	AG1
Number of Residues	12
Details	binding site for residue CHD O 302

Chain	Residue
C	PEK306
G	ARG14
G	ARG17
G	GLY22
N	MET271
O	GLU62
O	THR63
O	HOH425
O	HOH431
O	HOH451
O	HOH459
O	HOH471

site_id	AG2
Number of Residues	11
Details	binding site for residue PSC O 303

Chain	Residue
N	PHE321
N	HIS328
O	MET56
O	ASP57
O	GLU60
O	TRP65
O	HOH532
R	GLU6
R	ASP8
V	ARG10
V	HOH170

site_id	AG3
Number of Residues	12
Details	binding site for residue PGV P 301

Chain	Residue
G	ALA1
N	PHE237
N	ASP298
P	TRP99
P	HIS103
P	ALA107
P	CHD307
P	HOH403
P	HOH412
P	HOH523
U	ASN24
U	HOH135

site_id	AG4
Number of Residues	17
Details	binding site for residue PGV P 303

Chain	Residue
P	VAL61
P	SER65
P	THR66
P	ILE210
P	PHE214
P	ARG221
P	HIS226
P	PHE227
P	THR228
P	HIS231
P	PHE233
P	GLY234
P	CDL304
P	HOH427
P	HOH444
P	HOH448
P	HOH509

site_id	AG5
Number of Residues	15
Details	binding site for residue CDL P 304

Chain	Residue
P	THR48
P	MET51
P	MET54
P	TYR55
P	ARG59
P	ILE62
P	ARG63
P	PHE67
P	PHE220
P	LYS224
P	HIS226
P	PGV303
P	HOH408
P	HOH502
P	HOH515

site_id	AG6
Number of Residues	9
Details	binding site for residue CHD P 305

Chain	Residue
P	ARG156
P	LEU160
P	GLN161
P	PHE164
P	PHE219
P	LEU223
P	HOH510
P	HOH571
W	PHE1

site_id	AG7
Number of Residues	8
Details	binding site for residue DMU P 306

Chain	Residue
N	LEU110
P	MET33
P	PHE37
P	HOH404
W	SER46
W	TYR48
W	CYS49
W	TRP52

site_id	AG8
Number of Residues	13
Details	binding site for residue CHD P 307

Chain	Residue
N	HIS233
N	ASP300
N	THR301
N	TYR304
N	HOH741
N	HOH913
P	TRP99
P	HIS103
P	PGV301
P	HOH442
P	HOH447
P	HOH513
P	HOH523

site_id	AG9
Number of Residues	17
Details	binding site for residue PEK P 308

Chain	Residue
A	SER279
A	ILE311
B	THR66
B	CHD303
P	LYS157
P	HIS158
P	GLN161
P	THR168
P	TYR172
P	HOH436
P	HOH441
P	HOH476
S	ALA1
T	ARG17
T	PHE21
T	GLY22
T	CDL103

site_id	AH1
Number of Residues	11
Details	binding site for residue PGV Q 201

Chain	Residue
N	ASN406
N	THR408
N	TRP409
N	ILE412
Q	PHE87
Q	HOH406
X	HIS10
X	HOH116
Z	GLN15
Z	LEU19
Z	SER20

site_id	AH2
Number of Residues	12
Details	binding site for residue TGL Q 202

Chain	Residue
N	TRP334
N	PHE414
N	HOH707
O	ILE42
O	THR47
O	HOH571
Q	ARG73
Q	THR75
Q	GLU77
Q	TRP78
V	ARG16
V	HIS20

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

Chain	Residue
S	CYS60
S	CYS62
S	CYS82
S	CYS85

site_id	AH4
Number of Residues	19
Details	binding site for residue PEK T 101

Chain	Residue
N	HIS151
N	ALA203
N	PGV607
P	TRP34
P	TYR181
P	TYR182
P	ALA184
P	PHE186
P	THR187
P	ILE188
P	PHE198
P	GLY205
T	TRP62
T	THR68
T	PHE69
T	PHE70
T	HIS71
T	ASN76
T	HOH237

site_id	AH5
Number of Residues	11
Details	binding site for residue PEK T 102

Chain	Residue
C	LYS77
C	ARG80
C	TYR81
C	PHE98
C	TRP240
C	VAL247
T	SER2
T	ALA3
T	LYS5
T	GLY6
T	CDL103

site_id	AH6
Number of Residues	23
Details	binding site for residue CDL T 103

Chain	Residue
A	ILE286
A	ASP300
A	SER307
A	ILE311
A	HOH730
B	ALA70
B	ALA77
B	TYR85
B	HOH476
P	LEU127
P	LEU131
P	SER135
P	LEU138
P	PEK308
T	SER27
T	LEU30
T	CYS31
T	ASN34
T	LEU37
T	HIS38
T	PEK102
T	HOH210
T	HOH244

site_id	AH7
Number of Residues	4
Details	binding site for residue CHD W 101

Chain	Residue
N	PHE8
W	TYR32
W	ARG33
W	THR37

site_id	AH8
Number of Residues	16
Details	binding site for residue TGL Y 101

Chain	Residue
N	THR17
N	LEU18
N	PHE22
N	TRP25
N	LEU113
N	PHE400
Y	PRO12
Y	PHE13
Y	SER14
Y	ARG20
Y	MET24
Y	PHE28
Y	PHE29
Y	SER31
Y	HOH221
Y	HOH225

site_id	AH9
Number of Residues	8
Details	binding site for residue DMU Z 101

Chain	Residue
Q	TRP98
Z	LEU28
Z	GLY31
Z	TRP32
Z	TYR35
Z	HIS36
Z	HOH206
Z	HOH225

site_id	AI1
Number of Residues	18
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	VAL287
N	HIS290
N	ILE312
N	HEA602
N	CU603
N	PER606

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	20
Details	TOPO_DOM: Mitochondrial matrix => ECO:0000269\|PubMed:27605664

Chain	Residue	Details
M	ILE1-SER11
N	SER262-GLY269
N	SER401-ASN406
N	LYS479-LYS514
Z	ILE1-SER11
F	CYS82
F	CYS85
S	CYS60
S	CYS62
S	CYS82
S	CYS85
N	MET171-PRO182

site_id	SWS_FT_FI2
Number of Residues	46
Details	TRANSMEM: Helical => ECO:0000269\|PubMed:27605664

Chain	Residue	Details
M	PRO12-TYR35
Z	PRO12-TYR35
F	LYS90
S	LYS37
S	LYS55
S	LYS90

site_id	SWS_FT_FI3
Number of Residues	20
Details	TOPO_DOM: Mitochondrial intermembrane => ECO:0000269\|PubMed:27605664

Chain	Residue	Details
M	HIS36-ALA46
Z	HIS36-ALA46
C	ALA184-ASP190
C	TYR257-SER261
P	PHE35-MET40
P	LEU106-GLU128
P	ALA184-ASP190
P	TYR257-SER261

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P17665

Chain	Residue	Details
L	LYS9
Y	LYS9
Q	LYS7
Q	LYS38

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P13073

Chain	Residue	Details
D	LYS31
O	CYS200
O	HIS204
O	MET207
Q	LYS31
B	GLU198
B	CYS200
B	HIS204
B	MET207
O	HIS161
O	CYS196
O	GLU198

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P10888

Chain	Residue	Details
D	SER34
D	SER36
Q	SER34
Q	SER36
N	ARG213-ASP227
N	VAL287-ASP298

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P19783

Chain	Residue	Details
D	LYS45
Q	LYS45

site_id	SWS_FT_FI8
Number of Residues	64
Details	TRANSMEM: Helical; Name=VI => ECO:0000269\|PubMed:27605664

Chain	Residue	Details
C	GLY191-LEU223
P	GLY191-LEU223

site_id	SWS_FT_FI9
Number of Residues	46
Details	TRANSMEM: Helical; Name=VII => ECO:0000269\|PubMed:27605664

Chain	Residue	Details
C	PHE233-ILE256
P	PHE233-ILE256

site_id	SWS_FT_FI10
Number of Residues	32
Details	TRANSMEM: Helical; Name=VII => ECO:0000269\|PubMed:27605664

Chain	Residue	Details
A	TYR270-ILE286
N	TYR270-ILE286

site_id	SWS_FT_FI11
Number of Residues	56
Details	TRANSMEM: Helical; Name=VIII => ECO:0000269\|PubMed:27605664

Chain	Residue	Details
A	VAL299-LEU327
N	VAL299-LEU327

site_id	SWS_FT_FI12
Number of Residues	14
Details	TOPO_DOM: Mitochondrial matrix => ECO:0000269\|PubMed:27605664

Chain	Residue	Details
A	HIS328-SER335
N	HIS328-SER335

site_id	SWS_FT_FI13
Number of Residues	42
Details	TRANSMEM: Helical; Name=IX => ECO:0000269\|PubMed:27605664

Chain	Residue	Details
A	PRO336-VAL357
N	PRO336-VAL357

site_id	SWS_FT_FI14
Number of Residues	48
Details	TOPO_DOM: Mitochondrial intermembrane => ECO:0000269\|PubMed:27605664

Chain	Residue	Details
A	LEU358-THR370
A	SER434-ALA446
N	LEU358-THR370
N	SER434-ALA446

site_id	SWS_FT_FI15
Number of Residues	58
Details	TRANSMEM: Helical; Name=X => ECO:0000269\|PubMed:27605664

Chain	Residue	Details
A	TYR371-PHE400
N	TYR371-PHE400

site_id	SWS_FT_FI16
Number of Residues	52
Details	TRANSMEM: Helical; Name=XI => ECO:0000269\|PubMed:27605664

Chain	Residue	Details
A	ASP407-LEU433
N	ASP407-LEU433

site_id	SWS_FT_FI17
Number of Residues	62
Details	TRANSMEM: Helical; Name=XII => ECO:0000269\|PubMed:27605664

Chain	Residue	Details
A	TYR447-SER478
N	TYR447-SER478

site_id	SWS_FT_FI18
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:27605664, ECO:0000305\|PubMed:23537388

Chain	Residue	Details
A	GLU40
A	GLY45
A	SER441
N	GLU40
N	GLY45
N	SER441

site_id	SWS_FT_FI19
Number of Residues	6
Details	BINDING: axial binding residue => ECO:0000269\|PubMed:20385840, ECO:0000269\|PubMed:8638158

Chain	Residue	Details
A	HIS61
A	HIS376
A	HIS378
N	HIS61
N	HIS376
N	HIS378

site_id	SWS_FT_FI20
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269\|PubMed:20385840, ECO:0000269\|PubMed:8638158

Chain	Residue	Details
A	HIS240
N	ASP369
A	HIS290
A	HIS291
A	HIS368
A	ASP369
N	HIS240
N	HIS290
N	HIS291
N	HIS368

site_id	SWS_FT_FI21
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	TYR244
N	TYR244

site_id	SWS_FT_FI22
Number of Residues	2
Details	MOD_RES: N-formylmethionine => ECO:0000269\|PubMed:2165784

Chain	Residue	Details
A	FME1
N	FME1

site_id	SWS_FT_FI23
Number of Residues	4
Details	CROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr) => ECO:0000269\|PubMed:10338009

Chain	Residue	Details
A	HIS240
A	TYR244
N	HIS240
N	TYR244

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)