Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3OMN

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

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	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	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 802

Chain	Residue
A	HEA2
A	CU15
A	HIS284
A	VAL287
A	HIS334
A	HOH701

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMU A 1005

Chain	Residue
A	PHE502
A	TRD553
A	HOH810
A	MET56
A	GLN61
A	PHE62

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMU A 7

Chain	Residue
A	TRP20
A	VAL31
A	MET443
A	SER444
A	HOH724

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE TRD A 1013

Chain	Residue
A	SER79

site_id	AC5
Number of Residues	29
Details	BINDING SITE FOR RESIDUE HEA A 1

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	MET460
A	PHE468
A	GLN471
A	ARG481
A	ARG482
A	SER504
A	PHE508
A	HOH730
A	HOH773
A	HOH775

site_id	AC6
Number of Residues	35
Details	BINDING SITE FOR RESIDUE HEA A 2

Chain	Residue
A	HOH15
A	TRP172
A	TRP280
A	VAL287
A	TYR288
A	VAL291
A	HIS333
A	HIS334
A	THR352
A	ALA356
A	THR359
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	HOH701
A	HOH717
A	HOH718
A	HOH784
A	OH802
B	ILE68
B	PRO108

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE TRD A 553

Chain	Residue
A	LEU80
A	TRP81
A	PRO82
A	DMU1005

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TRD A 3

Chain	Residue
A	ARG476
B	THR41

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 A 5

Chain	Residue
A	HIS284
A	HIS333
A	HIS334
A	HOH701
A	OH802

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

Chain	Residue
A	HIS411
A	ASP412
A	HOH801
B	GLU254
B	HOH503
B	HOH801

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 554

Chain	Residue
A	GLU54
A	ALA57
A	GLY59
A	GLN61
A	HOH803
A	HOH810

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 10

Chain	Residue
A	HIS26
A	MET133

site_id	BC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE DMU B 1

Chain	Residue
A	TRP451
A	LEU509
A	TYR517
B	DMU2
B	HOH26
B	GLN142
B	TRP143
B	PRO164
B	HOH403
B	HOH413
B	HOH728
B	HOH790

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMU B 2

Chain	Residue
A	TRP451
A	ALA506
A	HOH769
B	DMU1

site_id	BC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE DMU B 3

Chain	Residue
A	TRP371
B	HIS96
B	ASN97
B	TRP104
B	HOH434
C	GLU86
C	HOH618
D	SER173
D	PRO174
D	GLU177

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMU B 6

Chain	Residue
B	PRO121
B	PHE124
B	GLU128
B	HOH493

site_id	BC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE TRD B 4

Chain	Residue
B	VAL113

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE HTH B 286

Chain	Residue
B	GLU152
B	ALA276
B	GLU280
B	HOH720
D	ALA276
D	GLU280
D	HIS283

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 B 287

Chain	Residue
B	CYS252
B	GLU254
B	CYS256
B	HIS260
B	CU1288

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 B 288

Chain	Residue
B	HIS217
B	CYS252
B	CYS256
B	MET263
B	CU1287

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B 8

Chain	Residue
B	GLU280
B	HIS283
B	HIS285
D	GLU152

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD B 9

Chain	Residue
B	HIS96
B	GLU101
B	HOH733
B	HOH768
B	HOH769

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OH C 802

Chain	Residue
C	HEA2
C	HIS284
C	VAL287
C	HIS334
C	CU1553
C	HOH701

site_id	CC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE DMU C 5

Chain	Residue
C	TRP451

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMU C 9

Chain	Residue
C	MET443
C	HOH602

site_id	CC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DMU C 10

Chain	Residue
C	MET56
C	ALA57
C	GLN61
C	SER83
C	PHE502
C	PHE505
C	TRD552
C	HOH580

site_id	CC9
Number of Residues	29
Details	BINDING SITE FOR RESIDUE HEA C 1

Chain	Residue
C	HOH3
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	MET424
C	SER425
C	VAL429
C	MET460
C	PHE468
C	GLN471
C	ARG481
C	ARG482
C	SER504
C	HOH581
C	HOH611

site_id	DC1
Number of Residues	33
Details	BINDING SITE FOR RESIDUE HEA C 2

Chain	Residue
C	HOH15
C	TRP172
C	TRP280
C	VAL287
C	TYR288
C	VAL291
C	HIS333
C	HIS334
C	THR352
C	ALA356
C	THR359
C	GLY360
C	PHE364
C	PHE391
C	THR392
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	HOH584
C	HOH600
C	HOH701
C	OH802

site_id	DC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE TRD C 552

Chain	Residue
C	DMU10
C	LEU80
C	TRP81
C	PRO82

site_id	DC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 C 553

Chain	Residue
C	HIS284
C	HIS333
C	HIS334
C	HOH701
C	OH802

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

Chain	Residue
C	HIS411
C	ASP412
D	GLU254
D	HOH311
D	HOH313
D	HOH314

site_id	DC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 7

Chain	Residue
C	GLU54
C	ALA57
C	GLY59
C	GLN61
C	HOH568
C	HOH580

site_id	DC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 554

Chain	Residue
C	HIS26
C	ALA132
C	MET133

site_id	DC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMU D 4

Chain	Residue
D	PRO121
D	PHE124
D	ASN125
D	GLU128

site_id	DC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMU D 8

Chain	Residue
D	PHE94
D	HIS96
D	ASN97

site_id	DC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TRD D 3

Chain	Residue
C	ARG476
D	THR41

site_id	EC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TRD D 14

Chain	Residue
C	MET353
D	LEU112

site_id	EC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 D 286

Chain	Residue
D	CYS252
D	GLU254
D	CYS256
D	HIS260
D	CU1287

site_id	EC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU1 D 287

Chain	Residue
D	HIS217
D	CYS252
D	CYS256
D	MET263
D	CU1286

site_id	EC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD D 288

Chain	Residue
B	GLU152
D	GLU280
D	HIS283
D	HIS285

site_id	EC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD D 9

Chain	Residue
D	HIS96
D	GLU101
D	HOH377
D	HOH378

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)