5A43
Crystal structure of a dual topology fluoride ion channel.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0016020 | cellular_component | membrane |
A | 0034220 | biological_process | monoatomic ion transmembrane transport |
A | 0046872 | molecular_function | metal ion binding |
A | 0062054 | molecular_function | fluoride channel activity |
A | 0140114 | biological_process | cellular detoxification of fluoride |
A | 1903424 | biological_process | fluoride transmembrane transport |
A | 1903425 | molecular_function | fluoride transmembrane transporter activity |
B | 0005886 | cellular_component | plasma membrane |
B | 0016020 | cellular_component | membrane |
B | 0034220 | biological_process | monoatomic ion transmembrane transport |
B | 0046872 | molecular_function | metal ion binding |
B | 0062054 | molecular_function | fluoride channel activity |
B | 0140114 | biological_process | cellular detoxification of fluoride |
B | 1903424 | biological_process | fluoride transmembrane transport |
B | 1903425 | molecular_function | fluoride transmembrane transporter activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 1127 |
Chain | Residue |
A | GLY75 |
A | SER78 |
A | THR79 |
B | GLY75 |
B | SER78 |
B | THR79 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE F B 1128 |
Chain | Residue |
B | PHE80 |
B | SER81 |
A | ASN41 |
A | GLY45 |
A | SER110 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE F A 1126 |
Chain | Residue |
A | SER81 |
B | ASN41 |
B | GLY45 |
B | SER110 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE DMU B 1129 |
Chain | Residue |
A | ALA115 |
A | PHE119 |
B | PHE88 |
B | LEU91 |
B | GLN92 |
B | GLY94 |
B | TYR96 |
C | PRO52 |
C | SER54 |
C | DMU1097 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMU A 1127 |
Chain | Residue |
A | LEU91 |
A | GLN92 |
A | GLY94 |
A | TYR96 |
B | PHE119 |
D | PRO52 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMU C 1097 |
Chain | Residue |
B | DMU1129 |
C | HIS32 |
C | THR50 |
C | PRO52 |
Functional Information from PROSITE/UniProt
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGNSP |
Chain | Residue | Details |
C | GLY38-PRO45 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 198 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:26344196, ECO:0007744|PDB:5A43 |
Chain | Residue | Details |
A | SER4-ASN27 | |
A | ASN32-PHE55 | |
A | PHE64-GLN92 | |
A | TYR96-ILE121 | |
B | SER4-ASN27 | |
B | ASN32-PHE55 | |
B | PHE64-GLN92 | |
B | TYR96-ILE121 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26344196, ECO:0007744|PDB:5A43 |
Chain | Residue | Details |
A | ASN41 | |
A | GLY75 | |
A | SER78 | |
A | SER110 | |
B | ASN41 | |
B | GLY75 | |
B | SER78 | |
B | SER110 |