Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3DTU

Catalytic core subunits (I and II) of cytochrome c oxidase from Rhodobacter sphaeroides complexed with deoxycholic acid

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	9
Details	BINDING SITE FOR RESIDUE DMU A 567

Chain	Residue
A	SER83
A	ALA84
A	ASN87
A	HOH1636
C	TRP371
D	LEU75
D	PHE94
D	HIS96
D	ASN97

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMU A 1004

Chain	Residue
A	TRP20
A	MET443
A	LEU512
A	HOH1560

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DMU A 1005

Chain	Residue
A	MET56
A	ALA57
A	GLN61
A	SER83
A	PHE502
A	PHE505
A	HOH1563
A	HOH1606

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMU B 1003

Chain	Residue
A	TRP371
B	HIS96
B	ASN97

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMU B 1011

Chain	Residue
B	PRO121
B	GLU128
B	HOH1182

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DMU C 567

Chain	Residue
C	MET56
C	GLN61
C	PHE62
C	SER83
C	PHE505
C	HOH642
C	HOH684

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMU C 568

Chain	Residue
A	GLU86
B	PRO174
C	TYR318
C	HOH718
C	HOH752

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMU D 11

Chain	Residue
D	PRO121
D	PHE124
D	GLU128

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 1023

Chain	Residue
A	HIS284
A	HIS333
A	HIS334
A	HOH1511

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1006

Chain	Residue
A	HIS411
A	ASP412
B	GLU254
B	HOH1064
B	HOH1070
B	HOH1077

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1007

Chain	Residue
A	GLU54
A	ALA57
A	GLY59
A	GLN61
A	HOH1550
A	HOH1563

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OH A 1501

Chain	Residue
A	HIS284
A	HIS334
A	HOH1511

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 1001

Chain	Residue
A	PHE135
A	PRO136
A	ARG137
A	MET138

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU B 1022

Chain	Residue
B	CYS252
B	GLU254
B	CYS256
B	HIS260

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU B 1004

Chain	Residue
B	HIS217
B	CYS252
B	CYS256
B	MET263

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B 1008

Chain	Residue
B	GLU280
B	HIS283
B	HIS285
D	GLU152

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B 1009

Chain	Residue
B	HIS96
B	GLU101
B	HOH1157
B	HOH1158

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B 1010

Chain	Residue
B	HIS284
B	HIS286
B	HOH1162
B	HOH1176

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU C 569

Chain	Residue
C	HIS284
C	HIS333
C	HIS334

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 570

Chain	Residue
C	HIS411
C	ASP412
C	HOH628
D	GLU254
D	HOH321
D	HOH333

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 571

Chain	Residue
C	HOH642
C	GLU54
C	ALA57
C	GLY59
C	GLN61
C	HOH629

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OH C 572

Chain	Residue
C	HIS284
C	HIS334
C	HOH589

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 573

Chain	Residue
C	PHE135
C	PRO136
C	ARG137
C	MET138

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU D 3

Chain	Residue
D	CYS252
D	GLU254
D	CYS256
D	HIS260

site_id	CC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU D 4

Chain	Residue
D	HIS217
D	CYS252
D	CYS256
D	MET263

site_id	CC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD D 8

Chain	Residue
B	GLU152
D	GLU280
D	HIS283
D	HIS285

site_id	CC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD D 9

Chain	Residue
C	HOH719
D	HIS96
D	GLU101

site_id	DC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEA A 1502

Chain	Residue
A	LEU34
A	THR48
A	MET51
A	ARG52
A	TRP95
A	ILE99
A	HIS102
A	MET106
A	MET107
A	GLY171
A	TRP172
A	TYR414
A	PHE420
A	HIS421
A	MET424
A	SER425
A	MET460
A	PHE468
A	GLN471
A	ARG481
A	ARG482
A	SER504
A	HOH1507
A	HOH1509
A	HOH1573

site_id	DC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEA A 1503

Chain	Residue
A	TRP172
A	TRP280
A	TYR288
A	HIS333
A	HIS334
A	THR352
A	ILE355
A	THR359
A	GLY360
A	GLY395
A	GLY398
A	LEU401
A	SER402
A	ASP407
A	HIS411
A	HIS419
A	PHE420
A	MET424
A	ARG481
A	HOH1511
A	HOH1520
A	HOH1527
A	HOH1536
A	HOH1556

site_id	DC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE TRD A 1504

Chain	Residue
A	TRP451
A	GLY513
A	TYR517

site_id	DC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TRD A 1505

Chain	Residue
A	LEU80
A	TRP81

site_id	DC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE TRD A 1506

Chain	Residue
A	ARG476
B	THR41
B	GLY42

site_id	DC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TRD A 1013

Chain	Residue
A	PHE76
A	SER79

site_id	DC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE TRD B 1012

Chain	Residue
B	PHE71

site_id	DC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE HTO B 1

Chain	Residue
B	ALA276
B	GLU280
B	HIS283
B	HOH1160
B	HOH1178
D	GLU152
D	ALA276
D	GLU280
D	HIS283
D	HOH298

site_id	DC9
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEA C 574

Chain	Residue
C	LEU34
C	THR48
C	MET51
C	ARG52
C	TRP95
C	ILE99
C	HIS102
C	MET106
C	MET107
C	GLY171
C	TRP172
C	TYR414
C	PHE420
C	HIS421
C	MET424
C	SER425
C	PHE468
C	GLN471
C	ARG481
C	ARG482
C	SER504
C	PHE508
C	HOH585
C	HOH587
C	HOH652

site_id	EC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEA C 575

Chain	Residue
C	TRP172
C	TRP280
C	TYR288
C	HIS333
C	THR352
C	ILE355
C	THR359
C	GLY360
C	GLY395
C	GLY398
C	ILE399
C	LEU401
C	SER402
C	ASP407
C	HIS411
C	HIS419
C	PHE420
C	MET424
C	ARG481
C	HOH589
C	HOH598
C	HOH605
C	HOH614
C	HOH635

site_id	EC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE DXC C 576

Chain	Residue
C	PRO315
C	TYR318
C	ALA319
C	ALA322
C	PRO358
C	ILE361
C	HOH718
C	HOH720
C	HOH721
D	HIS96
D	GLU101

site_id	EC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TRD C 577

Chain	Residue
C	MET443
C	SER444

site_id	EC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TRD C 579

Chain	Residue
C	TYR50
C	PHE76

site_id	EC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE TRD C 583

Chain	Residue
C	HIS223
C	LYS224
C	ASP536

site_id	EC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE TRD C 584

Chain	Residue
C	HIS127
C	HIS300
C	ALA303
C	THR304
C	PHE438
C	HIS534
C	ALA535
C	ASP536
C	THR537
C	GLU539
C	TRP540
C	HOH686
C	HOH701

site_id	EC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE TRD D 7

Chain	Residue
C	ARG476
D	THR41
D	GLY42
D	THR69

site_id	EC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE TRD D 12

Chain	Residue
D	PHE71

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)