Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005247 | molecular_function | voltage-gated chloride channel activity |
A | 0006821 | biological_process | chloride transport |
A | 0016020 | cellular_component | membrane |
A | 0055085 | biological_process | transmembrane transport |
B | 0005247 | molecular_function | voltage-gated chloride channel activity |
B | 0006821 | biological_process | chloride transport |
B | 0016020 | cellular_component | membrane |
B | 0055085 | biological_process | transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue DMU A 501 |
Chain | Residue |
A | THR9 |
A | DMU502 |
B | PHE388 |
B | SER402 |
B | ALA403 |
A | LEU14 |
A | GLY18 |
A | GLU88 |
A | LYS140 |
A | TYR141 |
A | SER143 |
A | THR144 |
A | HIS180 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue DMU A 502 |
Chain | Residue |
A | GLU8 |
A | THR9 |
A | LEU14 |
A | HIS179 |
A | HIS180 |
A | LEU183 |
A | DMU501 |
B | PHE388 |
B | LYS391 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue DMU A 503 |
Chain | Residue |
A | PHE388 |
A | LYS391 |
B | THR9 |
B | LEU14 |
B | HIS179 |
B | HIS180 |
B | DMU501 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue DMU A 504 |
Chain | Residue |
A | LEU214 |
A | ILE216 |
A | PRO217 |
A | PHE219 |
B | THR191 |
B | THR194 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue F A 505 |
Chain | Residue |
A | GLY116 |
A | ARG117 |
A | GLU118 |
A | GLY119 |
A | GLY317 |
A | VAL319 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue F A 506 |
Chain | Residue |
A | GLU318 |
A | TYR396 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue DMU B 501 |
Chain | Residue |
A | DMU503 |
B | LEU17 |
B | GLU88 |
B | TYR141 |
B | SER143 |
B | THR144 |
B | LYS176 |
B | HIS180 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue DMU B 502 |
Chain | Residue |
B | PHE251 |
B | TRP256 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue F B 503 |
Chain | Residue |
B | GLY116 |
B | ARG117 |
B | GLU118 |
B | GLY119 |
B | GLY317 |
B | VAL319 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue F B 504 |
Chain | Residue |
B | GLY119 |
B | GLU318 |
B | TYR396 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue MHA C 101 |
Chain | Residue |
C | TYR38 |
C | PHE50 |
C | THR60 |
C | SER62 |
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 |
D | GLY39-PRO46 | |