4KKC
Structure of the E148A mutant of CLC-ec1 deltaNC construct in 20mM Bromide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005247 | molecular_function | voltage-gated chloride channel activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006821 | biological_process | chloride transport |
| A | 0015297 | molecular_function | antiporter activity |
| A | 0016020 | cellular_component | membrane |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0062158 | molecular_function | chloride:proton antiporter activity |
| A | 1902476 | biological_process | chloride transmembrane transport |
| A | 1902600 | biological_process | proton transmembrane transport |
| A | 1990451 | biological_process | cellular stress response to acidic pH |
| B | 0005247 | molecular_function | voltage-gated chloride channel activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0006821 | biological_process | chloride transport |
| B | 0015297 | molecular_function | antiporter activity |
| B | 0016020 | cellular_component | membrane |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0055085 | biological_process | transmembrane transport |
| B | 0062158 | molecular_function | chloride:proton antiporter activity |
| B | 1902476 | biological_process | chloride transmembrane transport |
| B | 1902600 | biological_process | proton transmembrane transport |
| B | 1990451 | biological_process | cellular stress response to acidic pH |
Functional Information from PROSITE/UniProt
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH |
| Chain | Residue | Details |
| D | TYR191-HIS197 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 432 |
| Details | TRANSMEM: Helical |
| Chain | Residue | Details |
| A | LEU33-VAL69 | |
| A | ILE422-PHE438 | |
| B | LEU33-VAL69 | |
| B | LEU77-TYR100 | |
| B | TRP124-GLY141 | |
| B | ALA148-PHE166 | |
| B | ILE215-PHE232 | |
| B | TRP253-HIS281 | |
| B | ILE288-ALA309 | |
| B | MET330-SER349 | |
| B | GLY355-VAL376 | |
| A | LEU77-TYR100 | |
| B | ILE422-PHE438 | |
| A | TRP124-GLY141 | |
| A | ALA148-PHE166 | |
| A | ILE215-PHE232 | |
| A | TRP253-HIS281 | |
| A | ILE288-ALA309 | |
| A | MET330-SER349 | |
| A | GLY355-VAL376 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 106 |
| Details | TOPO_DOM: Periplasmic |
| Chain | Residue | Details |
| A | HIS70-PRO76 | |
| A | ASN233-LEU252 | |
| A | PRO310-SER329 | |
| A | GLU377-ALA386 | |
| B | HIS70-PRO76 | |
| B | ASN233-LEU252 | |
| B | PRO310-SER329 | |
| B | GLU377-ALA386 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 104 |
| Details | INTRAMEM: Helical |
| Chain | Residue | Details |
| A | ILE109-LEU116 | |
| B | PRO405-THR416 | |
| A | LEU177-ALA189 | |
| A | PRO193-ILE201 | |
| A | GLY387-SER401 | |
| A | PRO405-THR416 | |
| B | ILE109-LEU116 | |
| B | LEU177-ALA189 | |
| B | PRO193-ILE201 | |
| B | GLY387-SER401 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 64 |
| Details | TOPO_DOM: Cytoplasmic |
| Chain | Residue | Details |
| A | GLU117-ARG123 | |
| A | ARG167-THR176 | |
| A | GLU202-SER214 | |
| A | ARG282-ASN287 | |
| B | GLU117-ARG123 | |
| B | ARG167-THR176 | |
| B | GLU202-SER214 | |
| B | ARG282-ASN287 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | INTRAMEM: Note=Loop between two helices |
| Chain | Residue | Details |
| A | ILE402-ALA404 | |
| A | ASP417-LEU421 | |
| B | ILE402-ALA404 | |
| B | ASP417-LEU421 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12649487, ECO:0000305|PubMed:16341087, ECO:0000305|PubMed:18678918, ECO:0007744|PDB:1OTT, ECO:0007744|PDB:1OTU |
| Chain | Residue | Details |
| A | SER107 | |
| B | SER107 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12649487, ECO:0007744|PDB:1OTS, ECO:0007744|PDB:4ENE, ECO:0007744|PDB:6LSC |
| Chain | Residue | Details |
| A | ILE356 | |
| B | ILE356 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12649487, ECO:0007744|PDB:1OTT |
| Chain | Residue | Details |
| A | PHE357 | |
| B | PHE357 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12649487, ECO:0007744|PDB:1OTS, ECO:0007744|PDB:1OTT, ECO:0007744|PDB:1OTU, ECO:0007744|PDB:4ENE, ECO:0007744|PDB:6LSC |
| Chain | Residue | Details |
| A | TYR445 | |
| B | TYR445 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | SITE: Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport |
| Chain | Residue | Details |
| A | ALA148 | |
| B | ALA148 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | SITE: Mediates proton transfer from the protein to the inner aqueous phase |
| Chain | Residue | Details |
| A | GLU203 | |
| B | GLU203 |
