Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3OMI

Catalytic core subunits (I and II) of cytochrome C oxidase from Rhodobacter sphaeroides with D132A mutation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004129	molecular_function	cytochrome-c oxidase activity
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	0016491	molecular_function	oxidoreductase activity
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	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	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	0016491	molecular_function	oxidoreductase activity
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	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	6
Details	BINDING SITE FOR RESIDUE OH A 601

Chain	Residue
A	HIS284
A	VAL287
A	HIS334
A	HEA608
A	CU611
A	HOH744

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMU A 602

Chain	Residue
A	MET443
A	SER444
A	HOH730
A	TRP20
A	VAL31
A	LEU34

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMU A 603

Chain	Residue
A	MET56
A	ALA57
A	GLN61
A	PHE502
A	TRD609
A	HOH817

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TRD A 605

Chain	Residue
A	PHE76
A	SER79

site_id	AC5
Number of Residues	30
Details	BINDING SITE FOR RESIDUE HEA A 607

Chain	Residue
A	LEU34
A	GLY38
A	VAL45
A	THR48
A	MET51
A	ARG52
A	TRP95
A	ILE99
A	HIS102
A	MET106
A	MET107
A	VAL111
A	GLY171
A	TRP172
A	TYR414
A	PHE420
A	HIS421
A	MET424
A	SER425
A	VAL429
A	MET460
A	PHE468
A	GLN471
A	ARG481
A	ARG482
A	SER504
A	PHE508
A	HOH784
A	HOH786
A	HOH827

site_id	AC6
Number of Residues	30
Details	BINDING SITE FOR RESIDUE HEA A 608

Chain	Residue
A	TRP172
A	TRP280
A	VAL287
A	TYR288
A	HIS333
A	HIS334
A	THR352
A	ILE355
A	THR359
A	GLY360
A	GLY395
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	OH601
A	HOH708
A	HOH718
A	HOH727
A	HOH744
A	HOH794
B	ILE68

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE TRD A 609

Chain	Residue
A	LEU80
A	TRP81
A	DMU603

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TRD A 610

Chain	Residue
A	ARG476
B	THR41

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU A 611

Chain	Residue
A	HIS284
A	HIS333
A	HIS334
A	OH601
A	HOH744

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 612

Chain	Residue
A	HIS411
A	ASP412
B	GLU254
B	HOH428
B	HOH514
B	HOH518

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 613

Chain	Residue
A	GLN61
A	HOH810
A	HOH817
A	GLU54
A	ALA57
A	GLY59

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 614

Chain	Residue
A	HIS26
A	MET133
A	HOH828
A	HOH832

site_id	BC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE DMU B 301

Chain	Residue
A	PRO449
A	TRP451
A	PHE510
A	GLY513
B	GLN142
B	TRP143
B	PRO164
B	DMU302
B	HOH407
B	HOH409
B	HOH435
B	HOH506

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMU B 302

Chain	Residue
A	TRP451
A	ALA506
A	HOH780
B	DMU301

site_id	BC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE DMU B 303

Chain	Residue
A	TRP371
B	PHE94
B	HIS96
B	ASN97
B	LEU100
B	TRP104
B	HOH422
C	GLU86
D	SER173
D	PRO174
D	GLU177
D	HOH483

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMU B 304

Chain	Residue
B	PRO121
B	PHE124
B	GLU128

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE TRD B 305

Chain	Residue
B	LEU112
B	VAL113
B	GLY116
B	ALA117

site_id	BC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE HTH B 306

Chain	Residue
B	GLU152
B	ALA276
B	GLU280
B	HIS283
B	HOH431
D	ALA276
D	GLU280
D	HIS283

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU B 307

Chain	Residue
B	CYS252
B	GLU254
B	CYS256
B	HIS260
B	CU1308

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 B 308

Chain	Residue
B	HIS217
B	CYS252
B	CYS256
B	MET263
B	CU307

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B 309

Chain	Residue
B	GLU280
B	HIS283
B	HIS285
D	GLU152

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD B 310

Chain	Residue
B	HIS96
B	GLU101
B	HOH430
B	HOH482
B	HOH483

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OH C 601

Chain	Residue
C	HIS284
C	VAL287
C	HIS334
C	HEA606
C	CU608
C	HOH795

site_id	CC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DMU C 602

Chain	Residue
C	MET53
C	MET56
C	GLN61
C	SER83
C	PHE502
C	PHE505
C	TRD607
C	HOH735

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMU C 604

Chain	Residue
C	MET443
C	SER444

site_id	CC8
Number of Residues	28
Details	BINDING SITE FOR RESIDUE HEA C 605

Chain	Residue
C	LEU34
C	GLY38
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	MET424
C	SER425
C	VAL429
C	MET460
C	PHE468
C	GLN471
C	ARG481
C	ARG482
C	SER504
C	HOH701
C	HOH736
C	HOH766

site_id	CC9
Number of Residues	28
Details	BINDING SITE FOR RESIDUE HEA C 606

Chain	Residue
C	TRP172
C	TRP280
C	VAL287
C	TYR288
C	HIS333
C	HIS334
C	THR352
C	ILE355
C	THR359
C	GLY360
C	GLY395
C	GLY398
C	LEU401
C	SER402
C	ASP407
C	HIS411
C	VAL416
C	HIS419
C	PHE420
C	VAL423
C	MET424
C	ARG481
C	OH601
C	HOH708
C	HOH739
C	HOH744
C	HOH757
C	HOH795

site_id	DC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE TRD C 607

Chain	Residue
C	LEU80
C	TRP81
C	PRO82
C	DMU602

site_id	DC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU C 608

Chain	Residue
C	HIS284
C	HIS333
C	HIS334
C	OH601
C	HOH795

site_id	DC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 609

Chain	Residue
C	HIS411
C	ASP412
C	HOH721
D	GLU254
D	HOH436
D	HOH438

site_id	DC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 610

Chain	Residue
C	GLU54
C	ALA57
C	GLY59
C	GLN61
C	HOH722
C	HOH735

site_id	DC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 611

Chain	Residue
C	HIS26
C	ALA132
C	MET133

site_id	DC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMU D 301

Chain	Residue
D	PRO121
D	GLU128

site_id	DC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMU D 302

Chain	Residue
D	HIS96
D	ASN97

site_id	DC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TRD D 303

Chain	Residue
C	ARG476
D	THR41

site_id	DC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU D 305

Chain	Residue
D	CYS252
D	GLU254
D	CYS256
D	HIS260
D	CU1306

site_id	EC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 D 306

Chain	Residue
D	HIS217
D	CYS252
D	CYS256
D	MET263
D	CU305

site_id	EC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD D 307

Chain	Residue
B	GLU152
D	GLU280
D	HIS283
D	HIS285

site_id	EC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD D 308

Chain	Residue
D	HIS96
D	GLU101
D	HOH501
D	HOH502

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

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