Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5IY5

Electron transfer complex of cytochrome c and cytochrome c oxidase at 2.0 angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
1	0005515	molecular_function	protein binding
1	0005758	cellular_component	mitochondrial intermembrane space
1	0005829	cellular_component	cytosol
1	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
1	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
1	0006915	biological_process	apoptotic process
1	0008289	molecular_function	lipid binding
1	0009055	molecular_function	electron transfer activity
1	0020037	molecular_function	heme binding
1	0022904	biological_process	respiratory electron transport chain
1	0042802	molecular_function	identical protein binding
1	0046872	molecular_function	metal ion binding
1	0070069	cellular_component	cytochrome complex
1	0097190	biological_process	apoptotic signaling pathway
2	0005515	molecular_function	protein binding
2	0005758	cellular_component	mitochondrial intermembrane space
2	0005829	cellular_component	cytosol
2	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
2	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
2	0006915	biological_process	apoptotic process
2	0008289	molecular_function	lipid binding
2	0009055	molecular_function	electron transfer activity
2	0020037	molecular_function	heme binding
2	0022904	biological_process	respiratory electron transport chain
2	0042802	molecular_function	identical protein binding
2	0046872	molecular_function	metal ion binding
2	0070069	cellular_component	cytochrome complex
2	0097190	biological_process	apoptotic signaling pathway
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	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	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	4
Details	binding site for residue CU A 601

Chain	Residue
A	HIS240
A	HIS290
A	HIS291
A	PER606

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 602

Chain	Residue
B	HOH531
A	HIS368
A	ASP369
B	GLU198
B	HOH434
B	HOH436

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

Chain	Residue
A	GLU40
A	GLY45
A	SER441
A	HOH783

site_id	AC4
Number of Residues	31
Details	binding site for residue HEA A 604

Chain	Residue
A	ALA24
A	GLY27
A	MET28
A	THR31
A	SER34
A	ILE37
A	ARG38
A	TYR54
A	VAL58
A	HIS61
A	ALA62
A	MET65
A	VAL70
A	ILE73
A	GLY125
A	TRP126
A	TYR371
A	PHE377
A	HIS378
A	SER382
A	VAL386
A	PHE393
A	MET417
A	PHE425
A	GLN428
A	ARG438
A	ARG439
A	MET468
A	HOH735
A	HOH740
A	HOH749

site_id	AC5
Number of Residues	31
Details	binding site for residue HEA A 605

Chain	Residue
A	TRP126
A	TRP236
A	VAL243
A	TYR244
A	HIS290
A	HIS291
A	THR309
A	ILE312
A	ALA313
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	PER606
A	HOH750
A	HOH767
A	HOH772
A	HOH791
B	ILE34
B	PRO69
B	ILE72

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

Chain	Residue
A	HIS240
A	VAL243
A	HIS291
A	CU601
A	HEA605

site_id	AC7
Number of Residues	8
Details	binding site for residue PGV A 607

Chain	Residue
A	ASN406
A	TRP409
A	HOH701
A	HOH833
D	PHE87
K	PHE9
M	GLN15
M	HOH216

site_id	AC8
Number of Residues	15
Details	binding site for residue PGV A 608

Chain	Residue
C	GLU64
C	HIS71
C	GLY82
C	PEK303
C	PGV304
A	PHE94
A	PRO95
A	ARG96
A	MET97
A	HOH748
A	HOH759
C	HIS9
C	ASN50
C	TRP57
C	TRP58

site_id	AC9
Number of Residues	7
Details	binding site for residue TGL B 301

Chain	Residue
A	ASN422
A	LEU433
B	LEU28
B	PHE32
B	SER35
B	SER36
B	HOH465

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	8
Details	binding site for residue EDO B 303

Chain	Residue
A	TYR447
B	ALA2
B	GLN10
B	LEU136
B	PRO166
B	TYR193
B	HOH471
B	HOH483

site_id	AD3
Number of Residues	10
Details	binding site for residue CHD C 301

Chain	Residue
A	HIS233
A	ASP300
A	THR301
A	TYR304
C	TRP99
C	HIS103
C	PGV305
C	HOH497
C	HOH500
T	CDL101

site_id	AD4
Number of Residues	3
Details	binding site for residue NA C 302

Chain	Residue
C	HIS148
C	HIS232
C	GLU236

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

Chain	Residue
A	HIS151
A	VAL155
A	PGV608
C	TYR181
C	TYR182
C	ALA184
C	PHE186
C	THR187
C	ILE188
C	PHE198
C	GLY202
G	TRP62
G	THR68
G	PHE69
G	PHE70
G	HIS71
G	ASN76
G	HOH226

site_id	AD6
Number of Residues	20
Details	binding site for residue PGV C 304

Chain	Residue
A	PGV608
C	MET51
C	MET54
C	VAL61
C	SER65
C	THR66
C	GLU90
C	ILE210
C	PHE214
C	ARG221
C	HIS226
C	PHE227
C	HIS231
C	PHE233
C	GLY234
C	CDL306
C	HOH436
C	HOH438
C	HOH485
F	HOH227

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

Chain	Residue
A	ASP298
B	HOH529
C	TRP99
C	TYR102
C	HIS103
C	ALA107
C	CHD301
C	HOH427
C	HOH431
C	HOH502
H	ASN22
P	TRP258
T	CDL101
T	HOH241

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	ARG63
C	PHE67
C	THR213
C	PHE220
C	LYS224
C	HIS226
C	PGV304
C	HOH401
C	HOH406
C	HOH470
C	HOH471
C	HOH534
C	HOH536
J	LYS8

site_id	AD9
Number of Residues	4
Details	binding site for residue CHD C 307

Chain	Residue
C	ARG156
C	GLN161
C	PHE164
J	PHE1

site_id	AE1
Number of Residues	4
Details	binding site for residue EDO C 311

Chain	Residue
C	GLU111
C	HOH420
C	HOH506
H	HOH128

site_id	AE2
Number of Residues	11
Details	binding site for residue TGL D 201

Chain	Residue
A	TRP334
A	MET339
A	GLY343
B	LYS49
D	ARG73
D	GLU77
D	TRP78
D	HOH303
D	HOH306
D	HOH392
I	HIS20

site_id	AE3
Number of Residues	17
Details	binding site for residue PSC E 201

Chain	Residue
A	PHE321
B	LEU37
B	ILE41
B	HIS52
B	MET56
B	ASP57
B	GLU60
B	VAL61
B	TRP65
B	LEU68
B	HOH554
E	HIS5
E	GLU6
E	THR7
E	ASP8
E	PHE11
I	HOH221

site_id	AE4
Number of Residues	4
Details	binding site for residue EDO E 202

Chain	Residue
E	GLU102
E	HOH301
E	HOH307
E	HOH391

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	5
Details	binding site for residue EDO F 102

Chain	Residue
C	HIS231
C	HOH424
F	ASP9
F	GLU17
F	HOH221

site_id	AE7
Number of Residues	19
Details	binding site for residue CDL G 101

Chain	Residue
C	VAL142
C	HOH526
G	LEU23
G	SER27
G	LEU30
G	CYS31
G	ASN34
G	LEU37
G	HIS38
G	HOH202
G	HOH244
N	TYR304
N	SER307
N	ILE311
O	ALA77
O	LEU78
O	LEU81
O	TYR85
O	HOH465

site_id	AE8
Number of Residues	9
Details	binding site for residue CHD G 102

Chain	Residue
G	ARG14
G	ARG17
G	GLY22
G	HOH208
G	HOH216
N	MET271
N	TRP275
O	GLU62
O	THR63

site_id	AE9
Number of Residues	6
Details	binding site for residue EDO G 103

Chain	Residue
C	GLY120
G	ALA46
G	PHE47
G	ILE48
G	ARG54
G	HOH229

site_id	AF1
Number of Residues	3
Details	binding site for residue EDO I 101

Chain	Residue
I	TYR54
I	ASP55
I	GLU62

site_id	AF2
Number of Residues	5
Details	binding site for residue CHD J 101

Chain	Residue
J	TYR32
J	MET36
J	THR37
J	LEU40
J	HOH221

site_id	AF3
Number of Residues	12
Details	binding site for residue TGL L 101

Chain	Residue
A	THR17
A	TRP25
A	PHE400
L	PRO12
L	PHE13
L	SER14
L	ARG20
L	MET25
L	LEU27
L	PHE28
L	PHE29
L	SER31

site_id	AF4
Number of Residues	8
Details	binding site for residue DMU M 101

Chain	Residue
D	TRP98
M	LEU28
M	GLY31
M	TRP32
M	LEU34
M	TYR35
M	HIS36
M	HOH211

site_id	AF5
Number of Residues	4
Details	binding site for residue CU N 602

Chain	Residue
N	HIS240
N	HIS290
N	HIS291
N	PER607

site_id	AF6
Number of Residues	6
Details	binding site for residue MG N 603

Chain	Residue
N	HIS368
N	ASP369
O	GLU198
O	HOH414
O	HOH445
O	HOH512

site_id	AF7
Number of Residues	4
Details	binding site for residue NA N 604

Chain	Residue
N	GLU40
N	GLY45
N	SER441
N	HOH806

site_id	AF8
Number of Residues	32
Details	binding site for residue HEA N 605

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	MET390
N	PHE393
N	PHE425
N	GLN428
N	ARG438
N	ARG439
N	TYR440
N	VAL465
N	MET468
N	ILE472
N	HOH743
N	HOH766
N	HOH794

site_id	AF9
Number of Residues	28
Details	binding site for residue HEA N 606

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	GLY355
N	LEU358
N	ALA359
N	ASP364
N	HIS368
N	VAL373
N	HIS376
N	PHE377
N	VAL380
N	LEU381
N	ARG438
N	PER607
N	HOH715
N	HOH745
N	HOH785
N	HOH834
O	ILE34

site_id	AG1
Number of Residues	5
Details	binding site for residue PER N 607

Chain	Residue
N	HIS240
N	VAL243
N	HIS291
N	CU602
N	HEA606

site_id	AG2
Number of Residues	10
Details	binding site for residue TGL N 608

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

site_id	AG3
Number of Residues	16
Details	binding site for residue PGV N 612

Chain	Residue
N	PHE94
N	PRO95
N	ARG96
N	MET97
N	HOH730
N	HOH772
P	HIS9
P	ASN50
P	MET54
P	TRP57
P	TRP58
P	GLU64
P	HIS71
P	GLY82
P	PHE93
P	PEK303

site_id	AG4
Number of Residues	6
Details	binding site for residue EDO N 613

Chain	Residue
N	TYR260
N	TYR261
N	HIS395
N	HOH716
N	HOH731
Z	ILE1

site_id	AG5
Number of Residues	1
Details	binding site for residue EDO N 614

Chain	Residue
P	LEU22

site_id	AG6
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	AG7
Number of Residues	7
Details	binding site for residue CHD P 301

Chain	Residue
N	HIS233
N	ASP300
N	THR301
N	TYR304
P	TRP99
P	HIS103
P	PGV305

site_id	AG8
Number of Residues	4
Details	binding site for residue NA P 302

Chain	Residue
P	HIS148
P	HIS232
P	GLU236
P	HOH492

site_id	AG9
Number of Residues	20
Details	binding site for residue PEK P 303

Chain	Residue
N	HIS151
N	VAL155
N	PGV612
P	TYR181
P	TYR182
P	ALA184
P	PHE186
P	THR187
P	ILE188
P	PHE198
P	GLY202
P	PHE203
P	GLY205
P	HOH457
T	TRP62
T	THR68
T	PHE69
T	PHE70
T	HIS71
T	ASN76

site_id	AH1
Number of Residues	19
Details	binding site for residue PGV P 304

Chain	Residue
P	MET51
P	TRP58
P	VAL61
P	SER65
P	THR66
P	PHE86
P	ILE210
P	PHE214
P	ARG221
P	HIS226
P	PHE227
P	HIS231
P	HIS232
P	PHE233
P	GLY234
P	HOH418
P	HOH426
P	HOH476
S	HOH211

site_id	AH2
Number of Residues	8
Details	binding site for residue PGV P 305

Chain	Residue
P	TRP99
P	HIS103
P	ALA107
P	CHD301
P	HOH481
U	ASN24
U	HOH103
U	HOH136

site_id	AH3
Number of Residues	16
Details	binding site for residue CDL P 306

Chain	Residue
P	MET51
P	LEU52
P	TYR55
P	ARG59
P	ILE62
P	PHE67
P	THR213
P	ILE216
P	VAL217
P	PHE220
P	LYS224
P	HIS226
P	HOH401
P	HOH403
P	HOH411
P	HOH425

site_id	AH4
Number of Residues	5
Details	binding site for residue CHD P 307

Chain	Residue
P	ARG156
P	PHE164
P	LEU223
P	HOH504
W	PHE1

site_id	AH5
Number of Residues	11
Details	binding site for residue TGL Q 201

Chain	Residue
N	TRP334
N	PHE414
N	HOH737
O	ILE42
Q	THR75
Q	GLU77
Q	TRP78
Q	ILE89
Q	HOH310
V	ARG16
V	HIS20

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	5
Details	binding site for residue EDO S 102

Chain	Residue
P	HOH467
S	ASP9
S	GLU17
S	HOH221
S	HOH241

site_id	AH8
Number of Residues	19
Details	binding site for residue CDL T 101

Chain	Residue
A	PHE282
A	ILE286
A	ASP300
A	TYR304
A	ILE311
A	HOH911
A	HOH927
B	ALA70
B	ILE74
B	LEU78
B	LEU81
B	HOH533
C	CHD301
C	PGV305
P	LEU127
T	SER27
T	CYS31
T	ASN34
T	HIS38

site_id	AH9
Number of Residues	11
Details	binding site for residue CHD T 103

Chain	Residue
A	MET271
A	TRP275
B	THR63
B	THR66
T	ARG14
T	ARG17
T	PHE18
T	PHE21
T	GLY22
T	HOH205
T	HOH215

site_id	AI1
Number of Residues	18
Details	binding site for residue PSC V 101

Chain	Residue
N	PHE268
N	PHE321
N	ALA325
N	HIS328
O	MET45
O	HIS52
O	MET56
O	ASP57
O	VAL61
O	TRP65
O	LEU68
R	HIS5
R	ASP8
V	ARG10
V	LEU17
V	ARG18
V	HOH201
V	HOH212

site_id	AI2
Number of Residues	7
Details	binding site for residue CHD W 101

Chain	Residue
N	ILE3
N	PHE8
W	TYR32
W	ARG33
W	MET36
W	LEU40
W	HOH204

site_id	AI3
Number of Residues	9
Details	binding site for residue DMU Z 101

Chain	Residue
N	LEU35
N	PHE459
Q	TRP98
Q	HOH359
Z	LEU27
Z	LEU28
Z	GLY31
Z	TRP32
Z	HIS36

site_id	AI4
Number of Residues	5
Details	binding site for Di-peptide ACE 1 0 and GLY 1 1

Chain	Residue
1	ASP2
1	VAL3
1	GLU92
1	ASP93
1	ALA96

site_id	AI5
Number of Residues	21
Details	binding site for Di-peptide HEM 1 201 and CYS 1 14

Chain	Residue
1	PHE10
1	LYS13
1	ALA15
1	GLN16
1	CYS17
1	HIS18
1	THR28
1	PRO30
1	THR40
1	GLY41
1	TYR48
1	THR49
1	ASN52
1	TRP59
1	TYR67
1	LEU68
1	THR78
1	LYS79
1	MET80
1	ILE81
1	PHE82

site_id	AI6
Number of Residues	21
Details	binding site for Di-peptide HEM 1 201 and CYS 1 17

Chain	Residue
1	LYS13
1	CYS14
1	ALA15
1	GLN16
1	HIS18
1	THR28
1	GLY29
1	PRO30
1	THR40
1	GLY41
1	TYR48
1	THR49
1	ASN52
1	TRP59
1	TYR67
1	LEU68
1	THR78
1	LYS79
1	MET80
1	ILE81
1	PHE82

site_id	AI7
Number of Residues	1
Details	binding site for Di-peptide ACE 2 0 and GLY 2 1

Chain	Residue
2	ASP2

site_id	AI8
Number of Residues	21
Details	binding site for Di-peptide HEM 2 201 and CYS 2 17

Chain	Residue
2	LYS13
2	CYS14
2	ALA15
2	GLN16
2	HIS18
2	THR28
2	GLY29
2	LEU35
2	THR40
2	PHE46
2	TYR48
2	THR49
2	ASN52
2	TRP59
2	LEU68
2	THR78
2	LYS79
2	MET80
2	ILE81
2	PHE82
2	HOH317

site_id	AI9
Number of Residues	21
Details	binding site for Di-peptide HEM 2 201 and CYS 2 14

Chain	Residue
2	PHE10
2	LYS13
2	ALA15
2	GLN16
2	CYS17
2	HIS18
2	THR28
2	LEU35
2	THR40
2	PHE46
2	TYR48
2	THR49
2	ASN52
2	TRP59
2	LEU68
2	THR78
2	LYS79
2	MET80
2	ILE81
2	PHE82
2	HOH317

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

site_id	SWS_FT_FI38
Number of Residues	4
Details	Binding site: {"description":"covalent"}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"5545094","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	2
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	2
Details	Modified residue: {"description":"N-acetylglycine","evidences":[{"source":"PubMed","id":"14469771","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62894","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI43
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI44
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI45
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62897","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)