Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6NMF

SFX structure of reduced cytochrome c oxidase at room temperature

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	24
Details	binding site for residue HEA A 601

Chain	Residue
A	THR31
A	VAL70
A	GLY125
A	TRP126
A	TYR371
A	PHE377
A	HIS378
A	LEU381
A	SER382
A	PHE425
A	GLN428
A	SER34
A	ARG438
A	ARG439
A	VAL465
A	HOH712
A	HOH740
A	ILE37
A	ARG38
A	TYR54
A	VAL58
A	HIS61
A	ALA62
A	MET65

site_id	AC2
Number of Residues	28
Details	binding site for residue HEA A 602

Chain	Residue
A	TRP126
A	TRP236
A	VAL243
A	TYR244
A	ILE247
A	HIS290
A	HIS291
A	THR309
A	ILE312
A	GLY317
A	GLY352
A	GLY355
A	LEU358
A	ALA359
A	ASP364
A	HIS368
A	VAL373
A	HIS376
A	PHE377
A	VAL380
A	LEU381
A	ARG438
A	HOH709
A	HOH716
A	HOH725
A	HOH765
B	ILE34
B	ILE72

site_id	AC3
Number of Residues	3
Details	binding site for residue CU A 603

Chain	Residue
A	HIS240
A	HIS290
A	HIS291

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

Chain	Residue
A	HIS368
A	ASP369
B	GLU198
B	HOH401
B	HOH409
B	HOH458

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

Chain	Residue
A	GLU40
A	GLY45
A	SER441
A	HOH784

site_id	AC6
Number of Residues	13
Details	binding site for residue PGV A 606

Chain	Residue
A	PHE94
A	PRO95
A	ARG96
A	MET97
C	HIS9
C	MET27
C	ASN50
C	MET54
C	TRP57
C	TRP58
C	GLU64
C	HIS71
C	PEK302

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

Chain	Residue
A	ASN406
A	THR408
A	TRP409
A	HOH793
D	PHE87
M	LYS4
M	PRO12
M	GLN15

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

Chain	Residue
A	PHE2
A	THR17
A	LEU18
A	TRP25
A	PHE400
A	HOH722
L	ASN10
L	ILE11
L	PRO12
L	MET24
L	PHE29
L	HOH109

site_id	AC9
Number of Residues	25
Details	binding site for residue CDL A 609

Chain	Residue
A	TYR304
A	SER307
A	ILE311
A	HOH701
A	HOH718
A	HOH755
A	HOH820
B	ALA70
B	LEU78
B	TYR85
B	HOH464
C	HOH453
P	LEU131
P	PHE251
P	PEK309
P	HOH428
T	SER27
T	CYS31
T	ASN34
T	LEU37
T	HIS38
T	PEK101
T	HOH202
T	HOH220
A	ASP300

site_id	AD1
Number of Residues	5
Details	binding site for residue TGL B 301

Chain	Residue
A	LEU433
B	LEU28
B	HOH454
B	HOH467
I	ARG43

site_id	AD2
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	AD3
Number of Residues	8
Details	binding site for residue CHD B 303

Chain	Residue
B	GLN59
B	GLU62
B	THR63
B	HOH425
P	PEK309
T	ARG14
T	PHE18
T	GLY22

site_id	AD4
Number of Residues	9
Details	binding site for residue PSC B 304

Chain	Residue
A	PHE321
B	ILE41
B	MET45
B	ASP57
B	TRP65
B	LEU68
B	HOH408
E	ASP8
I	LEU17

site_id	AD5
Number of Residues	7
Details	binding site for residue DMU C 301

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

site_id	AD6
Number of Residues	17
Details	binding site for residue PEK C 302

Chain	Residue
A	HIS151
A	PGV606
C	TYR181
C	TYR182
C	ALA184
C	PHE186
C	THR187
C	ILE188
C	PHE198
C	HOH407
C	HOH447
G	TRP62
G	THR68
G	PHE69
G	PHE70
G	HIS71
G	ASN76

site_id	AD7
Number of Residues	11
Details	binding site for residue PGV C 303

Chain	Residue
C	SER65
C	THR66
C	ILE210
C	PHE214
C	ARG221
C	HIS226
C	PHE227
C	HIS231
C	PHE233
C	GLY234
F	HOH205

site_id	AD8
Number of Residues	10
Details	binding site for residue CDL C 304

Chain	Residue
C	MET51
C	TYR55
C	ARG63
C	PHE220
C	LYS224
C	HIS226
C	HOH426
J	LYS8
J	ASP28
J	HOH209

site_id	AD9
Number of Residues	4
Details	binding site for residue CHD C 305

Chain	Residue
C	ARG156
C	GLN161
C	PHE164
J	PHE1

site_id	AE1
Number of Residues	9
Details	binding site for residue CHD C 306

Chain	Residue
A	HIS233
A	ASP300
A	THR301
A	TYR304
C	TRP99
C	HIS103
C	PGV307
C	HOH430
C	HOH439

site_id	AE2
Number of Residues	11
Details	binding site for residue PGV C 307

Chain	Residue
A	HOH706
C	TRP99
C	TYR102
C	HIS103
C	LEU106
C	ALA107
C	CHD306
C	HOH429
C	HOH450
H	ASN24
H	HOH105

site_id	AE3
Number of Residues	8
Details	binding site for residue TGL D 201

Chain	Residue
A	TRP334
A	LYS411
A	ALA415
D	ARG73
D	THR75
D	GLU77
D	TRP78
I	HIS20

site_id	AE4
Number of Residues	4
Details	binding site for residue ZN F 101

Chain	Residue
F	CYS60
F	CYS62
F	CYS82
F	CYS85

site_id	AE5
Number of Residues	9
Details	binding site for residue PEK G 101

Chain	Residue
C	LYS157
C	HIS158
C	GLN161
C	HOH454
F	ALA1
G	ARG17
G	CDL102
G	CHD104
O	GLN59

site_id	AE6
Number of Residues	20
Details	binding site for residue CDL G 102

Chain	Residue
C	LEU127
C	LEU131
C	LEU138
C	HOH424
G	CYS31
G	ASN34
G	HIS38
G	PEK101
G	PEK103
G	HOH207
G	HOH218
N	PHE282
N	ASP300
N	TYR304
N	SER307
N	ILE311
O	LEU78
O	LEU81
O	TYR85
P	CHD307

site_id	AE7
Number of Residues	8
Details	binding site for residue PEK G 103

Chain	Residue
G	SER2
G	LYS5
G	HIS8
G	CDL102
G	HOH202
P	ILE84
P	TRP240
P	PHE251

site_id	AE8
Number of Residues	9
Details	binding site for residue CHD G 104

Chain	Residue
G	ARG14
G	ARG17
G	GLY22
G	PEK101
G	HOH201
N	MET271
O	GLN59
O	GLU62
O	THR63

site_id	AE9
Number of Residues	6
Details	binding site for residue CHD J 101

Chain	Residue
A	LEU7
J	TYR32
J	ARG33
J	THR37
J	LEU40
J	HOH205

site_id	AF1
Number of Residues	5
Details	binding site for residue DMU M 101

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

site_id	AF2
Number of Residues	23
Details	binding site for residue HEA N 601

Chain	Residue
N	THR31
N	SER34
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	MET417
N	PHE425
N	GLN428
N	ARG438
N	ARG439
N	TYR440
N	MET468
N	HOH714

site_id	AF3
Number of Residues	25
Details	binding site for residue HEA N 602

Chain	Residue
N	TRP126
N	TRP236
N	VAL243
N	TYR244
N	ILE247
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	ARG438
N	HOH701
N	HOH719
N	HOH737

site_id	AF4
Number of Residues	3
Details	binding site for residue CU N 603

Chain	Residue
N	HIS240
N	HIS290
N	HIS291

site_id	AF5
Number of Residues	5
Details	binding site for residue MG N 604

Chain	Residue
N	HIS368
N	ASP369
O	GLU198
O	HOH401
O	HOH422

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

Chain	Residue
N	GLU40
N	GLY45
N	SER441
N	HOH774

site_id	AF7
Number of Residues	9
Details	binding site for residue PGV N 606

Chain	Residue
N	ASN406
N	THR408
N	TRP409
N	HOH761
Q	ALA84
Q	PHE87
X	HIS10
Z	PRO12
Z	GLN15

site_id	AF8
Number of Residues	8
Details	binding site for residue TGL N 607

Chain	Residue
N	ILE332
N	TRP334
N	HOH762
O	LEU46
Q	GLU77
Q	TRP78
Q	MET86
V	ARG16

site_id	AF9
Number of Residues	10
Details	binding site for residue PSC N 608

Chain	Residue
N	PHE321
N	HIS328
O	ILE41
O	HIS52
O	MET56
O	ASP57
O	TRP65
R	THR7
R	ASP8
V	ARG10

site_id	AG1
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	AG2
Number of Residues	13
Details	binding site for residue PGV P 301

Chain	Residue
N	PHE94
N	PRO95
N	ARG96
N	MET97
N	HOH711
P	HIS9
P	ALA24
P	TRP57
P	TRP58
P	GLU64
P	HIS71
P	LEU79
P	HOH432

site_id	AG3
Number of Residues	8
Details	binding site for residue PGV P 302

Chain	Residue
G	ALA1
N	ASP298
P	TRP99
P	TYR102
P	HIS103
P	ALA107
P	CHD307
U	ASN22

site_id	AG4
Number of Residues	6
Details	binding site for residue DMU P 303

Chain	Residue
P	MET33
P	PHE37
W	SER46
W	CYS49
W	TRP52
W	ALA53

site_id	AG5
Number of Residues	17
Details	binding site for residue PGV P 304

Chain	Residue
P	TRP58
P	VAL61
P	SER65
P	THR66
P	ILE210
P	PHE214
P	ARG221
P	HIS226
P	PHE227
P	HIS231
P	HIS232
P	PHE233
P	GLY234
P	CDL305
P	HOH403
P	HOH410
P	HOH432

site_id	AG6
Number of Residues	16
Details	binding site for residue CDL P 305

Chain	Residue
P	MET51
P	TYR55
P	TRP58
P	ARG59
P	ILE62
P	ARG63
P	PHE67
P	VAL217
P	PHE220
P	ARG221
P	LYS224
P	HIS226
P	PGV304
P	HOH410
W	LYS8
W	THR27

site_id	AG7
Number of Residues	2
Details	binding site for residue CHD P 306

Chain	Residue
P	ARG156
P	PHE164

site_id	AG8
Number of Residues	7
Details	binding site for residue CHD P 307

Chain	Residue
G	CDL102
N	HIS233
N	THR301
N	TYR304
P	TRP99
P	HIS103
P	PGV302

site_id	AG9
Number of Residues	14
Details	binding site for residue PEK P 308

Chain	Residue
P	TYR181
P	TYR182
P	ALA184
P	PHE186
P	THR187
P	ILE188
P	PHE198
P	HOH402
P	HOH439
T	THR68
T	PHE69
T	PHE70
T	HIS71
T	ASN76

site_id	AH1
Number of Residues	5
Details	binding site for residue PEK P 309

Chain	Residue
A	CDL609
B	CHD303
P	GLN161
P	HOH431
T	ARG17

site_id	AH2
Number of Residues	6
Details	binding site for residue DMU Q 201

Chain	Residue
Q	LEU95
Q	TRP98
Q	TYR102
Z	LEU27
Z	LEU28
Z	TYR35

site_id	AH3
Number of Residues	5
Details	binding site for residue ZN S 101

Chain	Residue
S	CYS60
S	CYS62
S	CYS82
S	CYS85
S	THR87

site_id	AH4
Number of Residues	11
Details	binding site for residue PEK T 101

Chain	Residue
A	CDL609
C	ARG80
C	TYR81
C	TRP240
T	SER2
T	ALA3
T	LYS5
T	GLY6
T	HIS8
T	TPO11
T	HOH208

site_id	AH5
Number of Residues	8
Details	binding site for residue TGL V 101

Chain	Residue
N	ASN422
N	LEU433
O	LEU7
O	LEU28
O	PHE32
V	ARG43
V	HOH204
V	HOH212

site_id	AH6
Number of Residues	3
Details	binding site for residue CHD W 101

Chain	Residue
N	ILE3
W	ARG33
W	HOH204

site_id	AH7
Number of Residues	8
Details	binding site for residue TGL Y 101

Chain	Residue
N	THR17
N	PHE400
Y	PRO12
Y	PHE13
Y	MET24
Y	PHE28
Y	PHE29
Y	HOH201

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)