Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3WG7

A 1.9 angstrom radiation damage free X-ray structure of large (420KDa) protein by femtosecond crystallography

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	34
Details	BINDING SITE FOR RESIDUE HEA A 601

Chain	Residue
A	MET28
A	MET65
A	ILE66
A	VAL70
A	ILE73
A	GLY125
A	TRP126
A	TYR371
A	PHE377
A	HIS378
A	SER382
A	THR31
A	VAL386
A	MET390
A	PHE393
A	MET417
A	PHE425
A	GLN428
A	ARG438
A	ARG439
A	TYR440
A	SER458
A	SER34
A	VAL465
A	MET468
A	HOH704
A	HOH725
A	HOH732
A	ILE37
A	ARG38
A	TYR54
A	VAL58
A	HIS61
A	ALA62

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	PER606
A	HOH705
A	HOH712
A	HOH723
A	HOH731
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
A	HOH722
B	GLU198
B	HOH410
B	HOH411

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 605

Chain	Residue
A	GLU40
A	GLY45
A	SER441
A	HOH720

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	HOH776
C	HIS9
C	ALA24
C	ASN50
C	TRP57
C	TRP58
C	GLU64
C	HIS71
C	LEU79
C	GLY82
C	PEK302
C	PGV303

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PGV A 608

Chain	Residue
A	THR408
A	HOH778
A	HOH931
D	PHE87
K	PHE9
K	HIS10
M	PRO12
M	LEU19
M	HOH2316
A	ASN406

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TGL B 301

Chain	Residue
A	ASN422
A	PHE426
A	PHE430
A	LEU433
B	LEU7
B	LEU28
B	PHE32
B	SER35
B	LEU39

site_id	BC1
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	BC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CHD B 303

Chain	Residue
A	MET271
A	TRP275
B	GLN59
B	GLU62
B	THR63
B	THR66
B	HOH455
B	HOH508
P	PEK308
T	ARG14
T	ARG17
T	PHE21
T	GLY22

site_id	BC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PSC B 304

Chain	Residue
A	PHE321
B	ILE41
B	HIS52
B	MET56
B	ASP57
B	GLU60
B	HOH576
E	HIS5
E	ASP8
E	PHE11
E	LEU41
E	HOH217
I	ARG10

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA C 301

Chain	Residue
C	HIS148
C	HIS232
C	GLU236
C	HOH404

site_id	BC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PEK C 302

Chain	Residue
A	VAL155
A	ALA203
A	PGV607
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	HOH205

site_id	BC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PGV C 303

Chain	Residue
A	PGV607
C	MET54
C	VAL61
C	SER65
C	THR66
C	ILE210
C	PHE214
C	ARG221
C	HIS226
C	PHE227
C	HIS231
C	PHE233
C	GLY234
C	CDL304
C	HOH432
C	HOH447
C	HOH475
F	HOH207

site_id	BC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE CDL C 304

Chain	Residue
C	THR48
C	MET51
C	LEU52
C	MET54
C	TYR55
C	TRP58
C	ARG59
C	ILE62
C	ARG63
C	PHE67
C	SER212
C	THR213
C	ILE216
C	PHE220
C	ARG221
C	LYS224
C	HIS226
C	PGV303
C	HOH421
C	HOH500
C	HOH513
C	HOH537
J	LYS8
J	LEU31

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CHD C 305

Chain	Residue
C	ARG156
C	PHE164
C	PHE219
C	LEU223
C	HOH510
J	PHE1

site_id	BC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CHD C 306

Chain	Residue
A	HIS233
A	ASP300
A	THR301
A	TYR304
C	TRP99
C	HIS103
C	PGV308
C	HOH503
C	HOH535
P	LEU127

site_id	CC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PEK C 307

Chain	Residue
C	LYS157
C	HIS158
C	GLN161
C	HOH525
G	ARG17
G	GLY22
G	CDL101
G	CHD103
G	HOH231
N	SER279
N	ILE311
O	GLN59
O	HOH486

site_id	CC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PGV C 308

Chain	Residue
A	PHE237
C	THR95
C	TRP99
C	TYR102
C	HIS103
C	ALA107
C	CHD306
C	HOH523
C	HOH538
H	ASN24
T	ALA1

site_id	CC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE TGL D 201

Chain	Residue
A	TRP334
A	LEU342
A	GLY343
A	ALA415
A	PHE418
A	VAL419
A	HOH908
B	LEU46
B	THR47
B	LYS49
B	HOH452
D	ARG73
D	SER74
D	THR75
D	GLU77
D	TRP78
D	HOH401
I	ARG16
I	HIS20

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 101

Chain	Residue
F	CYS60
F	CYS62
F	CYS82
F	CYS85

site_id	CC5
Number of Residues	24
Details	BINDING SITE FOR RESIDUE CDL G 101

Chain	Residue
C	LEU127
C	LEU131
C	LEU138
C	VAL254
C	PEK307
C	HOH528
G	SER27
G	LEU30
G	ASN34
G	LEU37
G	HIS38
G	HOH231
G	HOH241
G	HOH265
N	PHE282
N	ILE286
N	ASP300
N	SER307
N	ILE311
N	ILE314
O	ALA70
O	LEU78
O	LEU81
O	TYR85

site_id	CC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PEK G 102

Chain	Residue
G	SER2
G	LYS5
G	GLY6
G	HOH236
G	HOH266
P	LYS77
P	ARG80
P	TYR81
P	VAL91
P	THR95
P	PHE98
P	TRP240
P	VAL247

site_id	CC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CHD G 103

Chain	Residue
C	PEK307
G	ARG14
G	ARG17
G	PHE21
G	GLY22
G	HOH211
G	HOH228
G	HOH263
N	MET271
N	TRP275
O	GLU62
O	THR63

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CHD J 101

Chain	Residue
A	ILE3
J	TYR32
J	ARG33
J	MET36
J	THR37

site_id	CC9
Number of Residues	13
Details	BINDING SITE FOR RESIDUE TGL L 101

Chain	Residue
A	THR17
A	PHE22
A	TRP25
A	PHE400
A	SER401
L	PRO12
L	PHE13
L	SER14
L	ARG20
L	MET24
L	PHE28
L	PHE29
L	SER31

site_id	DC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMU M 101

Chain	Residue
D	TRP98
M	LEU28
M	TRP32
M	TYR35
M	HIS36
M	HOH2331

site_id	DC2
Number of Residues	31
Details	BINDING SITE FOR RESIDUE HEA N 601

Chain	Residue
N	GLY27
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	PHE393
N	PHE425
N	GLN428
N	ARG438
N	ARG439
N	MET468
N	HOH704
N	HOH724
N	HOH731
N	HOH911
Y	TGL101

site_id	DC3
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	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	HOH705
N	HOH712
N	HOH722
N	HOH730
O	ILE34

site_id	DC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU N 603

Chain	Residue
N	HIS240
N	HIS290
N	HIS291
N	PER606

site_id	DC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG N 604

Chain	Residue
N	HIS368
N	ASP369
O	GLU198
O	HOH401
O	HOH411
O	HOH412

site_id	DC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA N 605

Chain	Residue
N	GLU40
N	GLY45
N	SER441
N	HOH720

site_id	DC7
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	DC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PGV N 607

Chain	Residue
N	ASN406
N	THR408
N	TRP409
Q	ALA84
Q	PHE87
X	PHE9
X	HIS10
Z	PRO12
Z	LEU19
Z	HOH222
Z	HOH223

site_id	DC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PGV N 608

Chain	Residue
N	PHE94
N	PRO95
N	ARG96
N	MET97
N	HOH775
N	HOH791
P	HIS9
P	ASN50
P	MET54
P	TRP57
P	TRP58
P	GLU64
P	HIS71
P	SER89
P	PEK303
P	PGV304
P	HOH499

site_id	EC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE TGL N 609

Chain	Residue
N	TYR379
N	ASN422
N	PHE426
N	LEU433
N	HOH899
N	HOH933
N	HOH940
O	LEU28
O	PHE32
O	SER35
O	LEU39
V	ARG43
V	HOH102

site_id	EC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PSC N 610

Chain	Residue
N	PHE321
N	LEU324
N	HIS328
N	HOH913
N	HOH948
O	ILE41
O	HIS52
O	ASP57
R	HIS5
R	ASP8
R	PHE11
R	HOH204
R	HOH232
R	HOH294
V	ARG10
V	HOH101

site_id	EC3
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	EC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PGV P 301

Chain	Residue
G	ALA1
N	HOH956
P	TYR102
P	HIS103
P	ALA107
P	CHD307
P	HOH512
U	ASN24
U	HOH123

site_id	EC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA P 302

Chain	Residue
P	HIS148
P	HIS232
P	GLU236

site_id	EC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PEK P 303

Chain	Residue
N	ALA203
N	PGV608
N	HOH953
P	TYR181
P	TYR182
P	ALA184
P	PHE186
P	THR187
P	ILE188
P	PHE198
P	HOH465
T	THR68
T	PHE69
T	PHE70
T	HIS71
T	ASN76

site_id	EC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE PGV P 304

Chain	Residue
N	PGV608
P	MET54
P	TRP58
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	CDL305
P	HOH429
P	HOH443
P	HOH475
P	HOH523
S	HOH208

site_id	EC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE CDL P 305

Chain	Residue
P	THR48
P	MET51
P	LEU52
P	MET54
P	TYR55
P	TRP58
P	ARG59
P	ILE62
P	ARG63
P	PHE67
P	ILE216
P	VAL217
P	PHE220
P	LYS224
P	HIS226
P	PGV304
P	HOH417
P	HOH451
P	HOH498
W	LEU31

site_id	EC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CHD P 306

Chain	Residue
P	ARG156
P	PHE164
P	PHE219
P	LEU223
W	PHE1

site_id	FC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CHD P 307

Chain	Residue
C	LEU127
N	HIS233
N	ASP300
N	THR301
N	TYR304
P	TRP99
P	HIS103
P	PGV301
P	HOH492

site_id	FC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PEK P 308

Chain	Residue
A	SER279
A	ILE311
B	CHD303
B	HOH582
P	LYS157
P	HIS158
P	GLN161
P	THR168
P	TYR172
P	HOH530
P	HOH539
S	ALA1
T	ARG17
T	GLY22
T	LEU25
T	CDL102

site_id	FC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TGL Q 201

Chain	Residue
N	TRP334
N	LEU342
N	GLY343
N	HOH890
O	LEU39
O	ILE42
O	THR47
O	THR48
O	HOH479
Q	ARG73
Q	GLU77
Q	TRP78

site_id	FC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN S 101

Chain	Residue
S	CYS60
S	CYS62
S	CYS82
S	CYS85

site_id	FC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PEK T 101

Chain	Residue
C	LYS77
C	ARG80
C	TYR81
C	ILE84
C	PHE98
C	TRP240
C	HOH529
C	HOH536
T	SER2
T	ALA3
T	LYS5
T	GLY6
T	HIS8
T	CDL102

site_id	FC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE CDL T 102

Chain	Residue
A	ASP300
A	ALA303
A	SER307
A	ALA308
A	ILE311
A	ILE314
B	LEU81
B	ARG82
B	TYR85
P	LEU127
P	LEU131
P	PEK308
P	HOH515
P	HOH529
T	SER27
T	LEU30
T	CYS31
T	ASN34
T	LEU37
T	HIS38
T	PEK101
T	HOH222
T	HOH238

site_id	FC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CHD W 101

Chain	Residue
W	TYR32
W	ARG33
W	MET36
W	THR37
W	HOH238

site_id	FC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE TGL Y 101

Chain	Residue
N	PHE2
N	THR17
N	LEU18
N	PHE22
N	TRP25
N	LEU113
N	PHE400
N	SER401
N	HEA601
Y	ASN10
Y	ILE11
Y	PRO12
Y	PHE13
Y	ARG20
Y	MET24
Y	MET25
Y	PHE28
Y	SER31
Y	HOH235

site_id	FC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DMU Z 101

Chain	Residue
N	PHE459
Q	TRP98
Z	LEU27
Z	LEU28
Z	TRP32
Z	TYR35
Z	HOH208
Z	HOH213

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)