Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3FYE

Catalytic core subunits (I and II) of cytochrome c oxidase from Rhodobacter sphaeroides in the reduced state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004129	molecular_function	cytochrome-c oxidase activity
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0006119	biological_process	oxidative phosphorylation
A	0006811	biological_process	monoatomic ion transport
A	0009060	biological_process	aerobic respiration
A	0015990	biological_process	electron transport coupled proton transport
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	0005515	molecular_function	protein binding
B	0005886	cellular_component	plasma 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	0042773	biological_process	ATP synthesis coupled electron transport
B	0046872	molecular_function	metal ion binding
B	1902600	biological_process	proton transmembrane transport
C	0004129	molecular_function	cytochrome-c oxidase activity
C	0005515	molecular_function	protein binding
C	0005886	cellular_component	plasma membrane
C	0006119	biological_process	oxidative phosphorylation
C	0006811	biological_process	monoatomic ion transport
C	0009060	biological_process	aerobic respiration
C	0015990	biological_process	electron transport coupled proton transport
C	0016020	cellular_component	membrane
C	0020037	molecular_function	heme binding
C	0022904	biological_process	respiratory electron transport chain
C	0045277	cellular_component	respiratory chain complex IV
C	0046872	molecular_function	metal ion binding
C	1902600	biological_process	proton transmembrane transport
D	0004129	molecular_function	cytochrome-c oxidase activity
D	0005507	molecular_function	copper ion binding
D	0005515	molecular_function	protein binding
D	0005886	cellular_component	plasma membrane
D	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0022900	biological_process	electron transport chain
D	0022904	biological_process	respiratory electron transport chain
D	0042773	biological_process	ATP synthesis coupled electron transport
D	0046872	molecular_function	metal ion binding
D	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE HEA A 567

Chain	Residue
A	LEU34
A	MET106
A	MET107
A	VAL111
A	GLY171
A	TRP172
A	TYR414
A	PHE420
A	HIS421
A	SER425
A	MET460
A	GLY38
A	PHE468
A	GLN471
A	ARG481
A	ARG482
A	SER504
A	PHE508
A	HOH583
A	HOH585
A	HOH649
A	VAL45
A	THR48
A	MET51
A	ARG52
A	TRP95
A	ILE99
A	HIS102

site_id	AC2
Number of Residues	30
Details	BINDING SITE FOR RESIDUE HEA A 568

Chain	Residue
A	TRP172
A	VAL287
A	VAL291
A	HIS333
A	HIS334
A	THR352
A	ALA356
A	GLY360
A	PHE364
A	PHE391
A	GLY395
A	VAL396
A	GLY398
A	ILE399
A	LEU401
A	SER402
A	ASP407
A	HIS411
A	VAL416
A	HIS419
A	PHE420
A	VAL423
A	MET424
A	ARG481
A	HOH595
A	HOH601
A	HOH603
A	HOH607
A	HOH635
A	HOH690

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU1 A 570

Chain	Residue
A	HIS284
A	HIS333
A	HIS334

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 571

Chain	Residue
A	HIS411
A	ASP412
B	GLU254
B	HOH326
B	HOH332
B	HOH338

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 572

Chain	Residue
A	GLU54
A	ALA57
A	GLY59
A	GLN61
A	HOH628
A	HOH640

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE DMU A 574

Chain	Residue
A	TRP451
A	LEU509
A	TYR517
A	DMU575
B	GLN142
B	TRP143
B	PRO164
B	HOH290
B	HOH303
B	HOH310
B	HOH323

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMU A 575

Chain	Residue
A	TRP451
A	ALA506
A	DMU574
A	HOH677

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMU A 576

Chain	Residue
A	TRP20
A	MET443
A	SER444

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE DMU A 577

Chain	Residue
A	HOH687
A	MET56
A	ALA57
A	GLN61
A	SER83
A	VAL85
A	PHE502
A	TRD578
A	HOH640

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE TRD A 578

Chain	Residue
A	LEU80
A	TRP81
A	DMU577

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE TRD A 579

Chain	Residue
A	ARG476
B	THR41
B	GLY42

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE HTO B 1

Chain	Residue
B	GLU152
B	ALA276
B	GLU280
B	HIS283
B	HOH292
D	ALA276
D	GLU280
D	HIS283
D	HOH1327

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 B 3

Chain	Residue
B	CU14
B	CYS252
B	GLU254
B	CYS256
B	HIS260

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 B 4

Chain	Residue
B	CU13
B	HIS217
B	CYS252
B	CYS256
B	MET263

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B 8

Chain	Residue
B	GLU280
B	HIS283
B	HIS285
D	GLU152

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD B 9

Chain	Residue
B	HIS96
B	GLU101
B	HOH393

site_id	BC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE DMU B 288

Chain	Residue
A	TRP371
B	PHE94
B	HIS96
B	ASN97
B	LEU100
B	TRP104
C	GLU86
D	PRO174
D	GLU177
D	HOH1151

site_id	BC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE TRD B 289

Chain	Residue
A	MET350

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMU B 11

Chain	Residue
B	LEU120
B	PRO121
B	PHE124
B	GLU128

site_id	CC2
Number of Residues	28
Details	BINDING SITE FOR RESIDUE HEA C 567

Chain	Residue
C	LEU34
C	GLY38
C	VAL45
C	THR48
C	MET51
C	ARG52
C	TRP95
C	ILE99
C	HIS102
C	MET106
C	MET107
C	VAL111
C	GLY171
C	TRP172
C	TYR414
C	PHE420
C	HIS421
C	SER425
C	VAL429
C	MET460
C	PHE468
C	GLN471
C	ARG482
C	SER504
C	PHE508
C	HOH1003
C	HOH1011
C	HOH1130

site_id	CC3
Number of Residues	29
Details	BINDING SITE FOR RESIDUE HEA C 568

Chain	Residue
C	TRP172
C	VAL287
C	VAL291
C	HIS333
C	HIS334
C	ALA356
C	GLY360
C	PHE364
C	PHE391
C	GLY395
C	VAL396
C	GLY398
C	ILE399
C	LEU401
C	SER402
C	ASP407
C	HIS411
C	VAL416
C	HIS419
C	PHE420
C	VAL423
C	MET424
C	ARG481
C	HOH1015
C	HOH1030
C	HOH1096
C	HOH1371
C	HOH1601
C	HOH1603

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU1 C 570

Chain	Residue
C	HIS284
C	HIS333
C	HIS334

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 571

Chain	Residue
C	HIS411
C	ASP412
C	HOH1082
D	GLU254
D	HOH1071
D	HOH1094

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 572

Chain	Residue
C	GLU54
C	ALA57
C	GLY59
C	GLN61
C	HOH1085
C	HOH1107

site_id	CC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE TRD C 1001

Chain	Residue
C	TRP451
C	GLY513
C	TYR517
C	DMU1002

site_id	CC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMU C 1002

Chain	Residue
C	TRP451
C	TRD1001

site_id	CC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE DMU C 1005

Chain	Residue
C	MET56
C	ALA57
C	GLN61
C	SER83
C	VAL85
C	PHE502
C	PHE505
C	TRD1006
C	HOH1107

site_id	DC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE TRD C 1006

Chain	Residue
C	LEU80
C	TRP81
C	DMU1005

site_id	DC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 D 3

Chain	Residue
D	CU14
D	CYS252
D	GLU254
D	CYS256
D	HIS260

site_id	DC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 D 4

Chain	Residue
D	CU13
D	HIS217
D	CYS252
D	CYS256
D	MET263

site_id	DC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD D 8

Chain	Residue
B	GLU152
D	GLU280
D	HIS283
D	HIS285

site_id	DC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD D 9

Chain	Residue
D	HIS96
D	GLU101
D	HOH1196
D	HOH1805

site_id	DC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DMU D 1003

Chain	Residue
C	TRP371
D	PHE71
D	LEU75
D	PHE94
D	HIS96
D	ASN97
D	TRP104

site_id	DC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TRD D 1007

Chain	Residue
C	ARG476
D	THR41

site_id	DC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE TRD D 1008

Chain	Residue
C	MET350

site_id	DC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMU D 1011

Chain	Residue
D	PRO121
D	GLU128

Functional Information from PROSITE/UniProt

site_id	PS00077
Number of Residues	55
Details	COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyiivlpafgivshviatfakkpifgylpmvyamvaigvlgfvvwa..HH

Chain	Residue	Details
A	TRP280-HIS334

site_id	PS00078
Number of Residues	49
Details	COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHswtvpafgvkqdavpgrlaqlwfraeregiffgq......CselCgisHayM

Chain	Residue	Details
B	VAL215-MET263

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	560
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ar1

Chain	Residue	Details
A	GLU286
A	LYS362

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ar1

Chain	Residue	Details
C	GLU286
C	LYS362

site_id	CSA3
Number of Residues	7
Details	Annotated By Reference To The Literature 1ar1

Chain	Residue	Details
A	HIS419
A	HIS421
A	ARG482
A	ARG481
A	PHE420
A	TYR288
A	HIS284

site_id	CSA4
Number of Residues	7
Details	Annotated By Reference To The Literature 1ar1

Chain	Residue	Details
C	HIS419
C	HIS421
C	ARG482
C	ARG481
C	PHE420
C	TYR288
C	HIS284

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)