Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XQS

Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0015078	molecular_function	proton transmembrane transporter activity
A	0015986	biological_process	proton motive force-driven ATP synthesis
A	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
A	0045263	cellular_component	proton-transporting ATP synthase complex, coupling factor F(o)
A	1902600	biological_process	proton transmembrane transport
B	0015078	molecular_function	proton transmembrane transporter activity
B	0015986	biological_process	proton motive force-driven ATP synthesis
B	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
B	0045263	cellular_component	proton-transporting ATP synthase complex, coupling factor F(o)
B	1902600	biological_process	proton transmembrane transport
C	0015078	molecular_function	proton transmembrane transporter activity
C	0015986	biological_process	proton motive force-driven ATP synthesis
C	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
C	0045263	cellular_component	proton-transporting ATP synthase complex, coupling factor F(o)
C	1902600	biological_process	proton transmembrane transport
D	0015078	molecular_function	proton transmembrane transporter activity
D	0015986	biological_process	proton motive force-driven ATP synthesis
D	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
D	0045263	cellular_component	proton-transporting ATP synthase complex, coupling factor F(o)
D	1902600	biological_process	proton transmembrane transport
E	0015078	molecular_function	proton transmembrane transporter activity
E	0015986	biological_process	proton motive force-driven ATP synthesis
E	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
E	0045263	cellular_component	proton-transporting ATP synthase complex, coupling factor F(o)
E	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CVM A 102

Chain	Residue
B	CVM102
E	CVM102

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM A 103

Chain	Residue
A	ALA63

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM A 104

Chain	Residue
E	CVM107

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CVM A 106

Chain	Residue
A	GLU62
B	CVM103

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM A 107

Chain	Residue
B	TYR67

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM A 108

Chain	Residue
A	VAL70

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM A 109

Chain	Residue
A	LEU73

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM A 110

Chain	Residue
B	CVM104

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CVM B 102

Chain	Residue
A	CVM102
B	ASN4
C	CVM102

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CVM B 103

Chain	Residue
A	GLU62
A	CVM106
B	ALA63

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CVM B 104

Chain	Residue
A	CVM110
B	ILE66

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CVM B 107

Chain	Residue
B	ILE66
B	CVM108

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CVM B 108

Chain	Residue
B	VAL70
B	CVM107

site_id	BC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM B 110

Chain	Residue
C	CVM104

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CVM C 102

Chain	Residue
B	CVM102
C	ASN4
C	LEU5
D	CVM102

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CVM C 103

Chain	Residue
B	GLU62
C	ALA63

site_id	BC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CVM C 104

Chain	Residue
B	CVM110
C	ILE66

site_id	BC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM C 106

Chain	Residue
C	ILE66

site_id	CC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM C 108

Chain	Residue
C	LEU73

site_id	CC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM C 109

Chain	Residue
C	LEU73

site_id	CC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CVM D 102

Chain	Residue
C	CVM102
D	ASN4
E	CVM102

site_id	CC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CVM D 104

Chain	Residue
D	ILE66
D	TYR67

site_id	CC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM D 106

Chain	Residue
D	ILE66

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CVM D 107

Chain	Residue
D	ILE66
D	CVM110
E	TYR67

site_id	CC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM D 108

Chain	Residue
D	VAL70

site_id	CC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM D 109

Chain	Residue
D	LEU73

site_id	CC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM D 110

Chain	Residue
D	CVM107

site_id	DC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CVM E 102

Chain	Residue
A	CVM102
D	CVM102
E	LEU5

site_id	DC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM E 103

Chain	Residue
E	ALA63

site_id	DC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CVM E 104

Chain	Residue
E	ILE66

site_id	DC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CVM E 107

Chain	Residue
A	CVM104
E	ILE66

Functional Information from PROSITE/UniProt

site_id	PS00605
Number of Residues	22
Details	ATPASE_C ATP synthase c subunit signature. ARQPeaegkIrGtlLLslaFmE

Chain	Residue	Details
A	ALA41-GLU62

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