Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1M56

Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)

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	0005886	cellular_component	plasma membrane
C	0009055	molecular_function	electron transfer activity
C	0009060	biological_process	aerobic respiration
C	0016020	cellular_component	membrane
C	0019646	biological_process	aerobic electron transport chain
C	0022904	biological_process	respiratory electron transport chain
C	1902600	biological_process	proton transmembrane transport
G	0004129	molecular_function	cytochrome-c oxidase activity
G	0005515	molecular_function	protein binding
G	0005886	cellular_component	plasma membrane
G	0006119	biological_process	oxidative phosphorylation
G	0006811	biological_process	monoatomic ion transport
G	0009060	biological_process	aerobic respiration
G	0015990	biological_process	electron transport coupled proton transport
G	0016020	cellular_component	membrane
G	0020037	molecular_function	heme binding
G	0022904	biological_process	respiratory electron transport chain
G	0045277	cellular_component	respiratory chain complex IV
G	0046872	molecular_function	metal ion binding
G	1902600	biological_process	proton transmembrane transport
H	0004129	molecular_function	cytochrome-c oxidase activity
H	0005507	molecular_function	copper ion binding
H	0005515	molecular_function	protein binding
H	0005886	cellular_component	plasma membrane
H	0016020	cellular_component	membrane
H	0016491	molecular_function	oxidoreductase activity
H	0022900	biological_process	electron transport chain
H	0022904	biological_process	respiratory electron transport chain
H	0042773	biological_process	ATP synthesis coupled electron transport
H	0046872	molecular_function	metal ion binding
H	1902600	biological_process	proton transmembrane transport
I	0004129	molecular_function	cytochrome-c oxidase activity
I	0005886	cellular_component	plasma membrane
I	0009055	molecular_function	electron transfer activity
I	0009060	biological_process	aerobic respiration
I	0016020	cellular_component	membrane
I	0019646	biological_process	aerobic electron transport chain
I	0022904	biological_process	respiratory electron transport chain
I	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU B 1003

Chain	Residue
B	CYS252
B	GLU254
B	CYS256
B	HIS260
B	CU1004

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU B 1004

Chain	Residue
B	CU1003
B	HIS217
B	CYS252
B	CYS256
B	MET263

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU A 1005

Chain	Residue
A	HIS284
A	HIS333
A	HIS334

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 2006

Chain	Residue
A	HIS411
A	ASP412
A	HOH2060
B	GLU254
B	HOH1007
B	HOH1010

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1007

Chain	Residue
A	GLU54
A	ALA57
A	PRO58
A	GLY59
A	GLN61
A	HOH2061

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU H 1003

Chain	Residue
H	CYS252
H	GLU254
H	CYS256
H	HIS260
H	CU1004

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU H 1004

Chain	Residue
H	HIS217
H	CYS252
H	CYS256
H	MET263
H	CU1003

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU G 1005

Chain	Residue
G	HIS284
G	HIS333
G	HIS334

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG G 3006

Chain	Residue
G	HIS411
G	ASP412
G	HOH3061
G	HOH3114
H	GLU254
H	HOH1050
H	HOH1054

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA G 1007

Chain	Residue
G	GLU54
G	ALA57
G	PRO58
G	GLY59
G	GLN61
G	HOH3062

site_id	BC2
Number of Residues	29
Details	BINDING SITE FOR RESIDUE HEA A 1001

Chain	Residue
A	LEU34
A	GLY38
A	VAL45
A	THR48
A	ARG52
A	TRP95
A	ILE99
A	HIS102
A	GLY103
A	MET106
A	MET107
A	TRP172
A	TYR414
A	PHE420
A	HIS421
A	MET424
A	SER425
A	VAL429
A	ILE432
A	ILE436
A	THR467
A	PHE468
A	ARG481
A	ARG482
A	ALA501
A	SER504
A	PHE508
A	HOH2019
A	HOH2057

site_id	BC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEA A 1002

Chain	Residue
A	ARG481
A	HOH2015
A	HOH2023
A	HOH2050
B	ILE68
B	PRO108
A	TRP172
A	TRP280
A	VAL287
A	TYR288
A	HIS333
A	HIS334
A	ILE355
A	THR359
A	GLY360
A	PHE391
A	LEU401
A	SER402
A	ASP407
A	HIS411
A	VAL416
A	HIS419
A	PHE420
A	VAL423
A	MET424

site_id	BC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 3PE C 2008

Chain	Residue
C	TRP59
C	VAL62
C	VAL63
C	SER66
C	HIS71
C	PHE83
C	PHE86
C	PHE219
C	ARG226
C	HIS231
C	PHE232
C	VAL238
C	GLY239
C	HOH2040

site_id	BC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 3PE A 2009

Chain	Residue
A	PHE135
A	PRO136
A	ARG137
A	MET138
A	ALA199
A	ILE202
A	ALA247
C	LEU12
C	TRP58
C	TRP59
C	GLY82
C	PHE83
C	PHE86

site_id	BC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3PE C 2010

Chain	Residue
A	TRP331
A	GLN344
A	3PE2012
B	ARG234
C	VAL91
C	TRP99
C	LYS103
C	TYR107
C	PHE249
C	VAL252
C	VAL253
C	PHE256
C	3PE2013
D	ALA36
D	3PE2011

site_id	BC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 3PE D 2011

Chain	Residue
A	LEU241
A	GLN344
A	TYR347
A	3PE2012
C	TYR107
C	LEU255
C	PHE256
C	3PE2010
D	ILE39
D	LEU43
D	ALA47
D	ASN50
D	ALA51
D	HOH72

site_id	BC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 3PE A 2012

Chain	Residue
A	ARG216
A	THR221
A	MET222
A	TRP230
A	TRP237
A	VAL325
C	VAL91
C	3PE2010
D	LYS23
D	THR24
D	MET31
D	ALA35
D	3PE2011

site_id	BC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 3PE C 2013

Chain	Residue
C	ARG80
C	ILE84
C	HIS152
C	TRP245
C	3PE2010
D	PHE25
D	ALA36
D	VAL37

site_id	CC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE HEA G 1001

Chain	Residue
G	LEU34
G	GLY38
G	THR48
G	MET51
G	ARG52
G	TRP95
G	ILE99
G	HIS102
G	MET106
G	TRP172
G	TYR414
G	PHE420
G	HIS421
G	MET424
G	SER425
G	VAL429
G	ILE432
G	ILE436
G	THR467
G	PHE468
G	GLN471
G	ARG481
G	ARG482
G	ALA501
G	SER504
G	PHE508
G	HOH3020
G	HOH3058

site_id	CC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEA G 1002

Chain	Residue
G	TRP172
G	TRP280
G	VAL287
G	TYR288
G	HIS333
G	HIS334
G	ILE355
G	THR359
G	GLY360
G	PHE391
G	LEU401
G	SER402
G	ASP407
G	HIS411
G	HIS419
G	PHE420
G	VAL423
G	MET424
G	ARG481
G	HOH3024
G	HOH3051
H	ILE68
H	PRO108

site_id	CC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 3PE I 3008

Chain	Residue
I	MET55
I	TRP59
I	VAL62
I	VAL63
I	SER66
I	HIS71
I	PHE83
I	PHE86
I	PHE219
I	ARG226
I	HIS231
I	PHE232
I	HIS237
I	VAL238
I	GLY239
I	HOH3041

site_id	CC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 3PE G 3009

Chain	Residue
G	PHE135
G	PRO136
G	ARG137
G	MET138
G	ILE202
G	ALA247
I	LEU12
I	MET55
I	TRP58
I	TRP59
I	GLY82
I	PHE83
I	PHE86

site_id	CC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 3PE I 3010

Chain	Residue
G	PHE281
G	TRP331
G	GLN344
G	3PE3012
H	ARG234
I	VAL91
I	TRP99
I	LYS103
I	TYR107
I	PHE249
I	VAL252
I	VAL253
I	PHE256
I	3PE3013
I	HOH3044
J	ALA36
J	3PE3011

site_id	CC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 3PE J 3011

Chain	Residue
G	LEU241
G	PHE281
G	GLN344
G	TYR347
G	3PE3012
G	HOH3073
I	TYR107
I	LEU255
I	PHE256
I	3PE3010
J	ILE39
J	ALA47
J	ASN50
J	ALA51

site_id	CC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 3PE G 3012

Chain	Residue
G	ARG216
G	THR221
G	MET222
G	TRP230
G	TRP237
G	VAL325
I	VAL91
I	3PE3010
J	THR24
J	MET31
J	ALA35
J	3PE3011

site_id	CC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 3PE I 3013

Chain	Residue
I	ARG80
I	ILE87
I	HIS152
I	TRP245
I	3PE3010
J	PHE25
J	VAL37

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	7
Details	Annotated By Reference To The Literature 1ar1

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

site_id	CSA2
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	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ar1

Chain	Residue	Details
A	GLU286
A	LYS362

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1ar1

Chain	Residue	Details
G	GLU286
G	LYS362

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)