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 | |
