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5A43

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 1127
ChainResidue
AGLY75
ASER78
ATHR79
BGLY75
BSER78
BTHR79

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE F B 1128
ChainResidue
BPHE80
BSER81
AASN41
AGLY45
ASER110

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE F A 1126
ChainResidue
ASER81
BASN41
BGLY45
BSER110

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE DMU B 1129
ChainResidue
AALA115
APHE119
BPHE88
BLEU91
BGLN92
BGLY94
BTYR96
CPRO52
CSER54
CDMU1097

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DMU A 1127
ChainResidue
ALEU91
AGLN92
AGLY94
ATYR96
BPHE119
DPRO52

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMU C 1097
ChainResidue
BDMU1129
CHIS32
CTHR50
CPRO52

Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGNSP
ChainResidueDetails
CGLY38-PRO45

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues198
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:26344196, ECO:0007744|PDB:5A43
ChainResidueDetails
ASER4-ASN27
AASN32-PHE55
APHE64-GLN92
ATYR96-ILE121
BSER4-ASN27
BASN32-PHE55
BPHE64-GLN92
BTYR96-ILE121

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:26344196, ECO:0007744|PDB:5A43
ChainResidueDetails
AASN41
AGLY75
ASER78
ASER110
BASN41
BGLY75
BSER78
BSER110

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PDB entries from 2024-07-24

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