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5A40

Crystal structure of a dual topology fluoride ion channel.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
A0046872molecular_functionmetal ion binding
A0062054molecular_functionfluoride channel activity
A0140114biological_processcellular detoxification of fluoride
A1903424biological_processfluoride transmembrane transport
A1903425molecular_functionfluoride transmembrane transporter activity
B0005886cellular_componentplasma membrane
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
B0046872molecular_functionmetal ion binding
B0062054molecular_functionfluoride channel activity
B0140114biological_processcellular detoxification of fluoride
B1903424biological_processfluoride transmembrane transport
B1903425molecular_functionfluoride transmembrane transporter activity
C0005886cellular_componentplasma membrane
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
C0046872molecular_functionmetal ion binding
C0062054molecular_functionfluoride channel activity
C0140114biological_processcellular detoxification of fluoride
C1903424biological_processfluoride transmembrane transport
C1903425molecular_functionfluoride transmembrane transporter activity
D0005886cellular_componentplasma membrane
D0016020cellular_componentmembrane
D0034220biological_processmonoatomic ion transmembrane transport
D0046872molecular_functionmetal ion binding
D0062054molecular_functionfluoride channel activity
D0140114biological_processcellular detoxification of fluoride
D1903424biological_processfluoride transmembrane transport
D1903425molecular_functionfluoride transmembrane transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG F 1092
ChainResidue
BASP91
BCYS94
FTYR75

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG E 1092
ChainResidue
AASP91
ACYS94
EHIS81

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG G 1092
ChainResidue
CASP91
CCYS94
GHIS81

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG H 1092
ChainResidue
DASP91
DCYS94
HHIS81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues400
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:26344196, ECO:0007744|PDB:5A40, ECO:0007744|PDB:5NKQ
ChainResidueDetails
ALEU7-LYS29
CPRO36-ILE57
CALA65-CYS94
CTYR98-LEU126
DLEU7-LYS29
DPRO36-ILE57
DALA65-CYS94
DTYR98-LEU126
APRO36-ILE57
AALA65-CYS94
ATYR98-LEU126
BLEU7-LYS29
BPRO36-ILE57
BALA65-CYS94
BTYR98-LEU126
CLEU7-LYS29

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:26344196, ECO:0007744|PDB:5NKQ
ChainResidueDetails
AASN43
CTYR104
CSER108
CSER112
DASN43
DTYR104
DSER108
DSER112
ATYR104
ASER108
ASER112
BASN43
BTYR104
BSER108
BSER112
CASN43

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00454, ECO:0000269|PubMed:26344196, ECO:0007744|PDB:5NKQ
ChainResidueDetails
AGLY77
ATHR80
BGLY77
BTHR80
CGLY77
CTHR80
DGLY77
DTHR80

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PDB entries from 2024-07-24

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