Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2YEV

Structure of caa3-type cytochrome oxidase

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	0009055	molecular_function	electron transfer activity
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	0046872	molecular_function	metal ion binding
A	0070469	cellular_component	respirasome
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	0009055	molecular_function	electron transfer activity
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0020037	molecular_function	heme binding
B	0022900	biological_process	electron transport chain
B	0042773	biological_process	ATP synthesis coupled electron transport
B	0046872	molecular_function	metal ion binding
B	0070469	cellular_component	respirasome
B	1902600	biological_process	proton transmembrane transport
C	0016020	cellular_component	membrane
D	0004129	molecular_function	cytochrome-c oxidase activity
D	0005886	cellular_component	plasma membrane
D	0006119	biological_process	oxidative phosphorylation
D	0009055	molecular_function	electron transfer activity
D	0009060	biological_process	aerobic respiration
D	0015990	biological_process	electron transport coupled proton transport
D	0016020	cellular_component	membrane
D	0020037	molecular_function	heme binding
D	0022904	biological_process	respiratory electron transport chain
D	0046872	molecular_function	metal ion binding
D	0070469	cellular_component	respirasome
D	1902600	biological_process	proton transmembrane transport
E	0004129	molecular_function	cytochrome-c oxidase activity
E	0005507	molecular_function	copper ion binding
E	0005886	cellular_component	plasma membrane
E	0009055	molecular_function	electron transfer activity
E	0016020	cellular_component	membrane
E	0016491	molecular_function	oxidoreductase activity
E	0020037	molecular_function	heme binding
E	0022900	biological_process	electron transport chain
E	0042773	biological_process	ATP synthesis coupled electron transport
E	0046872	molecular_function	metal ion binding
E	0070469	cellular_component	respirasome
E	1902600	biological_process	proton transmembrane transport
F	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE 5PL A 900

Chain	Residue
A	LEU106
A	GLU601
A	ALA617
A	PHE624
A	LEU735
A	ILE742
A	PHE745
A	GLN753
A	LYS758
A	THR766
A	ALA769
A	ARG108
A	HOH2038
A	HOH2136
A	HOH2139
A	HOH2154
A	HOH2155
A	VAL109
A	PHE165
A	PHE568
A	LEU593
A	TRP596
A	ALA597
A	ASP600

site_id	AC2
Number of Residues	29
Details	BINDING SITE FOR RESIDUE HAS A 1015

Chain	Residue
A	PHE39
A	ALA40
A	GLY43
A	SER46
A	ILE49
A	ARG50
A	TYR66
A	LEU70
A	HIS73
A	GLY74
A	MET77
A	LEU78
A	GLY138
A	TRP139
A	TYR380
A	PHE386
A	HIS387
A	LEU390
A	MET391
A	PHE434
A	GLN437
A	ARG447
A	ARG448
A	TYR449
A	ALA470
A	LEU473
A	GLY474
A	HOH2029
A	HOH2111

site_id	AC3
Number of Residues	34
Details	BINDING SITE FOR RESIDUE HAS A 1016

Chain	Residue
A	TRP139
A	TRP246
A	VAL253
A	TYR254
A	HIS299
A	HIS300
A	THR318
A	ILE321
A	ALA322
A	GLY326
A	GLY361
A	ILE362
A	GLY364
A	VAL365
A	LEU367
A	SER368
A	ASP373
A	HIS377
A	VAL382
A	HIS385
A	PHE386
A	VAL389
A	LEU390
A	SER394
A	ARG447
A	HOH2077
A	HOH2091
A	HOH2096
A	HOH2100
A	HOH2112
B	PHE45
B	SER46
B	ILE49
B	LEU98

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU A 1017

Chain	Residue
A	HIS250
A	HIS299
A	HIS300
A	HOH2076
A	HOH2077

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 4AG A 1200

Chain	Residue
B	ALA23
B	THR25
A	MET366
A	ALA439
A	TYR442
A	LEU443
A	ALA457
A	TRP658
B	ARG21

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 7E8 A 1300

Chain	Residue
A	LEU29
A	MET409
A	THR410
A	PRO511
A	HOH2127

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 7E8 A 1301

Chain	Residue
A	GLN68
A	PHE129
A	HOH2032

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1801

Chain	Residue
A	HIS377
A	ASP378
A	HOH2044
A	HOH2101
A	HOH2102
B	GLU199

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CUA B 585

Chain	Residue
B	HIS162
B	CYS197
B	GLU199
B	CYS201
B	HIS205
B	MET208

site_id	BC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEC B 587

Chain	Residue
B	PHE126
B	TRP127
B	ASN141
B	ASN246
B	CYS247
B	CYS250
B	HIS251
B	PRO264
B	TRP269
B	ARG272
B	LEU275
B	GLY276
B	ALA277
B	LEU287
B	TRP290
B	ILE291
B	LYS298
B	VAL301
B	MET303
B	PRO304
B	LEU321
B	HOH2018
B	HOH2026
B	HOH2069

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 7E9 B 701

Chain	Residue
A	PHE665
B	HOH2090
D	LEU657
D	TRP658
D	LEU661
D	LEU662
D	PHE665

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 101

Chain	Residue
A	THR308

site_id	BC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE 5PL D 900

Chain	Residue
D	LEU106
D	ARG108
D	PHE165
D	LEU169
D	ALA590
D	LEU593
D	TRP596
D	ALA597
D	ASP600
D	GLU601
D	GLU628
D	LEU738
D	ILE742
D	PHE745
D	GLY746
D	GLN753
D	LYS758
D	GLY765
D	THR766
D	ALA769
D	TYR773
D	HOH2020
D	HOH2093
D	HOH2096
D	HOH2111

site_id	BC5
Number of Residues	26
Details	BINDING SITE FOR RESIDUE HAS D 1015

Chain	Residue
D	PHE37
D	PHE39
D	ALA40
D	GLY43
D	SER46
D	ILE49
D	ARG50
D	TYR66
D	LEU70
D	HIS73
D	MET77
D	LEU78
D	GLY138
D	TRP139
D	TYR380
D	PHE386
D	HIS387
D	MET391
D	PHE434
D	GLN437
D	ARG447
D	ARG448
D	TYR449
D	LEU473
D	HOH2012
D	HOH2082

site_id	BC6
Number of Residues	35
Details	BINDING SITE FOR RESIDUE HAS D 1016

Chain	Residue
D	TRP139
D	TRP246
D	VAL253
D	TYR254
D	HIS299
D	HIS300
D	THR318
D	ILE321
D	ALA322
D	GLY326
D	LEU358
D	GLY361
D	ILE362
D	GLY364
D	VAL365
D	LEU367
D	SER368
D	ASP373
D	HIS377
D	VAL382
D	HIS385
D	PHE386
D	VAL389
D	LEU390
D	SER394
D	ARG447
D	HOH2054
D	HOH2067
D	HOH2074
D	HOH2075
D	HOH2083
E	PHE45
E	ILE49
E	PRO91
E	LEU98

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU D 1017

Chain	Residue
D	HIS250
D	HIS299
D	HIS300
D	HOH2053
D	HOH2054

site_id	BC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL D 1701

Chain	Residue
D	SER771
D	HIS775

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 1801

Chain	Residue
D	HIS377
D	ASP378
D	HOH2027
D	HOH2070
D	HOH2076
E	GLU199

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CUA E 585

Chain	Residue
E	HIS162
E	CYS197
E	GLU199
E	CYS201
E	HIS205
E	MET208

site_id	CC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE HEC E 587

Chain	Residue
B	PRO307
E	PHE126
E	TRP127
E	ASN141
E	ASN246
E	CYS247
E	CYS250
E	HIS251
E	PRO264
E	TRP269
E	ARG272
E	LEU275
E	GLY276
E	ALA277
E	LEU287
E	TRP290
E	ILE291
E	LYS298
E	VAL301
E	MET303
E	PRO304
E	PHE306
E	LEU317
E	HOH2004
E	HOH2008
E	HOH2030

site_id	CC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL F 101

Chain	Residue
D	THR308

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. WFYSHPtVyvmllpylgilaevastfarkplfgyrqmvwaqmgivvlgtmvwa..HH

Chain	Residue	Details
A	TRP246-HIS300

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

Chain	Residue	Details
B	VAL160-MET208

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	720
Details	TRANSMEM: Helical => ECO:0000255

Chain	Residue	Details
A	LEU29-ILE49
A	PHE381-GLY401
A	PHE423-LEU443
A	LEU464-MET484
A	PHE566-LEU586
A	ALA617-ALA637
A	LEU657-ALA677
A	PHE691-PHE711
A	PHE729-LEU749
A	SER771-TRP791
D	LEU29-ILE49
A	LEU78-MET98
D	LEU78-MET98
D	ALA111-PRO131
D	PHE155-VAL175
D	ALA201-LEU221
D	PHE244-LEU264
D	MET282-PHE302
D	ILE312-ILE332
D	LEU347-LEU367
D	PHE381-GLY401
D	PHE423-LEU443
A	ALA111-PRO131
D	LEU464-MET484
D	PHE566-LEU586
D	ALA617-ALA637
D	LEU657-ALA677
D	PHE691-PHE711
D	PHE729-LEU749
D	SER771-TRP791
A	PHE155-VAL175
A	ALA201-LEU221
A	PHE244-LEU264
A	MET282-PHE302
A	ILE312-ILE332
A	LEU347-LEU367

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: axial binding residue => ECO:0000305

Chain	Residue	Details
A	HIS73
A	HIS385
A	HIS387
D	HIS73
D	HIS385
D	HIS387

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	HIS250
A	TYR254
D	HIS250
D	TYR254

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	HIS299
A	HIS300
D	HIS299
D	HIS300

site_id	SWS_FT_FI5
Number of Residues	4
Details	CROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr) => ECO:0000250

Chain	Residue	Details
A	HIS250
A	TYR254
D	HIS250
D	TYR254

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