Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1FFT

The structure of ubiquinol oxidase from Escherichia coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004129	molecular_function	cytochrome-c oxidase activity
A	0005507	molecular_function	copper ion binding
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0006811	biological_process	monoatomic ion transport
A	0009055	molecular_function	electron transfer activity
A	0009060	biological_process	aerobic respiration
A	0009319	cellular_component	cytochrome o ubiquinol oxidase complex
A	0009486	molecular_function	cytochrome bo3 ubiquinol oxidase activity
A	0015078	molecular_function	proton transmembrane transporter activity
A	0015453	molecular_function	oxidoreduction-driven active transmembrane transporter activity
A	0015990	biological_process	electron transport coupled proton transport
A	0016020	cellular_component	membrane
A	0016682	molecular_function	oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
A	0019646	biological_process	aerobic electron transport chain
A	0020037	molecular_function	heme binding
A	0022904	biological_process	respiratory electron transport chain
A	0046872	molecular_function	metal ion binding
A	0048039	molecular_function	ubiquinone binding
A	1902600	biological_process	proton transmembrane transport
B	0004129	molecular_function	cytochrome-c oxidase activity
B	0005507	molecular_function	copper ion binding
B	0009486	molecular_function	cytochrome bo3 ubiquinol oxidase activity
B	0016020	cellular_component	membrane
B	0016682	molecular_function	oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
B	0022900	biological_process	electron transport chain
C	0004129	molecular_function	cytochrome-c oxidase activity
C	0009055	molecular_function	electron transfer activity
C	0009486	molecular_function	cytochrome bo3 ubiquinol oxidase activity
C	0016020	cellular_component	membrane
C	0019646	biological_process	aerobic electron transport chain
C	0022904	biological_process	respiratory electron transport chain
F	0004129	molecular_function	cytochrome-c oxidase activity
F	0005507	molecular_function	copper ion binding
F	0005515	molecular_function	protein binding
F	0005886	cellular_component	plasma membrane
F	0006811	biological_process	monoatomic ion transport
F	0009055	molecular_function	electron transfer activity
F	0009060	biological_process	aerobic respiration
F	0009319	cellular_component	cytochrome o ubiquinol oxidase complex
F	0009486	molecular_function	cytochrome bo3 ubiquinol oxidase activity
F	0015078	molecular_function	proton transmembrane transporter activity
F	0015453	molecular_function	oxidoreduction-driven active transmembrane transporter activity
F	0015990	biological_process	electron transport coupled proton transport
F	0016020	cellular_component	membrane
F	0016682	molecular_function	oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
F	0019646	biological_process	aerobic electron transport chain
F	0020037	molecular_function	heme binding
F	0022904	biological_process	respiratory electron transport chain
F	0046872	molecular_function	metal ion binding
F	0048039	molecular_function	ubiquinone binding
F	1902600	biological_process	proton transmembrane transport
G	0004129	molecular_function	cytochrome-c oxidase activity
G	0005507	molecular_function	copper ion binding
G	0009486	molecular_function	cytochrome bo3 ubiquinol oxidase activity
G	0016020	cellular_component	membrane
G	0016682	molecular_function	oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
G	0022900	biological_process	electron transport chain
H	0004129	molecular_function	cytochrome-c oxidase activity
H	0009055	molecular_function	electron transfer activity
H	0009486	molecular_function	cytochrome bo3 ubiquinol oxidase activity
H	0016020	cellular_component	membrane
H	0019646	biological_process	aerobic electron transport chain
H	0022904	biological_process	respiratory electron transport chain

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU A 1003

Chain	Residue
A	HIS284
A	HIS333
A	HIS334

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU F 1003

Chain	Residue
F	HIS284
F	HIS333
F	HIS334

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM A 1001

Chain	Residue
A	PHE103
A	THR104
A	HIS106
A	GLY107
A	MET110
A	ILE111
A	GLY169
A	TRP170
A	ILE417
A	HIS421
A	ILE424
A	ILE425
A	VAL429
A	PHE468
A	ARG481
A	ARG482
A	PHE73
A	ARG80
A	TYR99

site_id	AC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEO A 1002

Chain	Residue
A	TRP280
A	VAL287
A	HIS333
A	HIS334
A	ALA356
A	THR359
A	GLY360
A	GLY395
A	GLY398
A	VAL399
A	LEU401
A	HIS411
A	ASN412
A	LEU416
A	HIS419
A	PHE420
A	VAL423
A	ILE424
A	ARG481
B	ILE56
B	PRO96
B	ILE99
B	ILE100

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM F 1001

Chain	Residue
F	PHE73
F	ARG80
F	TYR99
F	PHE103
F	THR104
F	HIS106
F	GLY107
F	MET110
F	ILE111
F	GLY169
F	TRP170
F	ILE417
F	HIS421
F	ILE424
F	ILE425
F	VAL429
F	PHE468
F	ARG481
F	ARG482

site_id	AC6
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEO F 1002

Chain	Residue
F	TRP170
F	TRP280
F	VAL287
F	HIS333
F	HIS334
F	ALA356
F	THR359
F	GLY360
F	GLY395
F	GLY398
F	VAL399
F	LEU401
F	HIS411
F	ASN412
F	LEU416
F	HIS419
F	PHE420
F	VAL423
F	ILE424
F	ARG481
G	ILE56
G	PRO96
G	ILE99
G	ILE100

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. WAWGHPeVyililpvfgvfseiaatfsrkrlfgytslvwatvcitvlsfivwl..HH

Chain	Residue	Details
A	TRP280-HIS334

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	54
Details	Transmembrane: {"description":"Helical; Name=II"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	142
Details	Topological domain: {"description":"Periplasmic"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	72
Details	Transmembrane: {"description":"Helical; Name=III"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	48
Details	Topological domain: {"description":"Cytoplasmic"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	46
Details	Transmembrane: {"description":"Helical; Name=IV"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	60
Details	Transmembrane: {"description":"Helical; Name=V"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	70
Details	Transmembrane: {"description":"Helical; Name=VI"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	72
Details	Transmembrane: {"description":"Helical; Name=VII"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	28
Details	Transmembrane: {"description":"Helical; Name=VIII"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	56
Details	Transmembrane: {"description":"Helical; Name=IX"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	62
Details	Transmembrane: {"description":"Helical; Name=X"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	64
Details	Transmembrane: {"description":"Helical; Name=XI"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	56
Details	Transmembrane: {"description":"Helical; Name=XII"}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	62
Details	Transmembrane: {"description":"Helical; Name=XIII"}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33408407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34417297","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WTI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CUW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7N9Z","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"34417297","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CUW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"34417297","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CUW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7N9Z","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	6
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11017202","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33408407","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FFT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WTI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11017202","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FFT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11017202","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33408407","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FFT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WTI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33408407","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WTI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	4
Details	Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"PubMed","id":"34417297","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	250
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	120
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	72
Details	Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	23
Details	a catalytic site defined by CSA, PubMed 11017202, 15598510, 12450405, 16624801, 9256439

Chain	Residue	Details
A	HIS419
A	THR201
A	SER145
A	MET79
A	ASN124
A	PHE420
A	PHE103
A	GLU286
A	THR149
A	HIS284
A	HIS421
A	LYS362
A	THR204
A	ASP75
A	ARG71
A	TYR288
A	ASP135
A	THR211
A	THR359
A	SER315
A	SER299
A	ASN142
A	TYR61

site_id	CSA2
Number of Residues	23
Details	a catalytic site defined by CSA, PubMed 11017202, 15598510, 12450405, 16624801, 9256439

Chain	Residue	Details
F	HIS419
F	THR201
F	SER145
F	MET79
F	ASN124
F	PHE420
F	PHE103
F	GLU286
F	THR149
F	HIS284
F	HIS421
F	LYS362
F	THR204
F	ASP75
F	ARG71
F	TYR288
F	ASP135
F	THR211
F	THR359
F	SER315
F	SER299
F	ASN142
F	TYR61

site_id	MCSA1
Number of Residues	23
Details	M-CSA 714

Chain	Residue	Details
A	TYR61	proton shuttle (general acid/base)
A	THR149	proton shuttle (general acid/base)
A	THR201	proton shuttle (general acid/base)
A	THR204	proton shuttle (general acid/base)
A	THR211	proton shuttle (general acid/base)
A	HIS284	metal ligand, modifies pKa
A	GLU286	proton shuttle (general acid/base)
A	TYR288	electron shuttle, proton shuttle (general acid/base)
A	SER299	proton shuttle (general acid/base)
A	SER315	proton shuttle (general acid/base)
A	THR359	proton shuttle (general acid/base)
A	ARG71	electrostatic stabiliser
A	LYS362	proton shuttle (general acid/base)
A	HIS419	electron shuttle
A	PHE420	electron shuttle
A	HIS421	electron shuttle
A	ASP75	electrostatic stabiliser
A	MET79	electron shuttle
A	PHE103	electron shuttle
A	ASN124	proton shuttle (general acid/base)
A	ASP135	proton shuttle (general acid/base)
A	ASN142	proton shuttle (general acid/base)
A	SER145	proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	23
Details	M-CSA 714

Chain

Residue

Details

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