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2XQU

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0015078molecular_functionproton transmembrane transporter activity
A0015986biological_processproton motive force-driven ATP synthesis
A0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
A0045263cellular_componentproton-transporting ATP synthase complex, coupling factor F(o)
A1902600biological_processproton transmembrane transport
B0015078molecular_functionproton transmembrane transporter activity
B0015986biological_processproton motive force-driven ATP synthesis
B0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
B0045263cellular_componentproton-transporting ATP synthase complex, coupling factor F(o)
B1902600biological_processproton transmembrane transport
C0015078molecular_functionproton transmembrane transporter activity
C0015986biological_processproton motive force-driven ATP synthesis
C0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
C0045263cellular_componentproton-transporting ATP synthase complex, coupling factor F(o)
C1902600biological_processproton transmembrane transport
D0015078molecular_functionproton transmembrane transporter activity
D0015986biological_processproton motive force-driven ATP synthesis
D0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
D0045263cellular_componentproton-transporting ATP synthase complex, coupling factor F(o)
D1902600biological_processproton transmembrane transport
E0015078molecular_functionproton transmembrane transporter activity
E0015986biological_processproton motive force-driven ATP synthesis
E0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
E0045263cellular_componentproton-transporting ATP synthase complex, coupling factor F(o)
E1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CVM A 102
ChainResidue
ASER3
AASN4
ALEU5
BLEU5
BCVM102
ESER3
ECVM102

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CVM A 103
ChainResidue
AALA63
EGLU62

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CVM A 104
ChainResidue
AILE66
ACVM108
ECVM107
ECVM110

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM A 106
ChainResidue
AILE66

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CVM A 107
ChainResidue
ACVM108
BTYR67

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CVM A 108
ChainResidue
AVAL70
ALEU73
ACVM104
ACVM107

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CVM A 109
ChainResidue
AVAL74
ACVM111
ECVM111

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM A 110
ChainResidue
ACVM111

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CVM A 111
ChainResidue
APHE77
ACVM109
ACVM110

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CVM A 112
ChainResidue
ALEU56
ELEU55

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CVM A 113
ChainResidue
AGLY52
ALEU55
AALA59
EARG51

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CVM B 102
ChainResidue
ASER3
ACVM102
BFME1
BASN4
BLEU5
BHOH2021
CCVM102

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CVM B 103
ChainResidue
AGLU62
BALA59
BALA63
BCVM112
BCVM113

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CVM B 104
ChainResidue
BALA63
BILE66
BTYR67

site_idBC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM B 106
ChainResidue
BALA59

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CVM B 107
ChainResidue
BCVM108
CTYR67

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CVM B 108
ChainResidue
BILE66
BLEU73
BCVM107
BCVM110
BCVM111

site_idBC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM B 109
ChainResidue
BCVM111

site_idCC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM B 110
ChainResidue
BCVM108

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CVM B 111
ChainResidue
BPHE77
BCVM108
BCVM109
CCVM109

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CVM B 112
ChainResidue
AARG51
ALEU55
BCVM103

site_idCC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CVM B 113
ChainResidue
AARG51
BGLY52
BLEU55
BCVM103

site_idCC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CVM C 102
ChainResidue
BFME1
BCVM102
CASN4
CLEU5
DLEU5
DCVM102

site_idCC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM C 103
ChainResidue
CALA63

site_idCC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM C 106
ChainResidue
CILE66

site_idCC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CVM C 107
ChainResidue
DTYR67
DCVM103
DCVM104

site_idCC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM C 108
ChainResidue
CVAL70

site_idDC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CVM C 109
ChainResidue
BCVM111
CVAL70
CLEU73

site_idDC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM C 110
ChainResidue
CCVM111

site_idDC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CVM C 111
ChainResidue
CPHE77
CCVM110
DVAL70
DCVM109

site_idDC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM C 112
ChainResidue
CCVM113

site_idDC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CVM C 113
ChainResidue
BARG51
CGLY52
CCVM112

site_idDC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CVM D 102
ChainResidue
DHOH2024
ECVM102
CSER3
CCVM102
DSER3
DASN4
DLEU5
DALA9

site_idDC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CVM D 103
ChainResidue
CGLU62
CCVM107
DALA63
DCVM112

site_idDC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CVM D 104
ChainResidue
CCVM107
DILE66

site_idDC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CVM D 107
ChainResidue
DCVM108
ETYR67

site_idEC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM D 108
ChainResidue
DCVM107

site_idEC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CVM D 109
ChainResidue
CCVM111
DLEU73

site_idEC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CVM D 110
ChainResidue
DLEU69
DCVM111

site_idEC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CVM D 111
ChainResidue
DPHE77
DCVM110
ECVM109

site_idEC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CVM D 112
ChainResidue
CARG51
DLEU56
DCVM103

site_idEC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CVM D 113
ChainResidue
CARG51
DGLY52
DLEU55
DALA59

site_idEC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CVM E 102
ChainResidue
ALEU5
ACVM102
DSER3
DCVM102
DHOH2001
EASN4
ELEU5

site_idEC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM E 103
ChainResidue
DGLU62

site_idEC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CVM E 104
ChainResidue
EILE66
ETYR67

site_idFC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM E 106
ChainResidue
EALA59

site_idFC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CVM E 107
ChainResidue
ACVM104
EILE66
ECVM108
ECVM110

site_idFC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CVM E 108
ChainResidue
EILE66
EVAL70
ECVM107

site_idFC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CVM E 109
ChainResidue
DCVM111

site_idFC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CVM E 110
ChainResidue
ACVM104
ECVM107

site_idFC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CVM E 111
ChainResidue
ACVM109
EPHE77

site_idFC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CVM E 113
ChainResidue
DARG51
EGLY52

Functional Information from PROSITE/UniProt
site_idPS00605
Number of Residues22
DetailsATPASE_C ATP synthase c subunit signature. ARQPeaegkIrGtlLLslaFmE
ChainResidueDetails
AALA41-GLU62

219140

PDB entries from 2024-05-01

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