1KPL
Crystal Structure of the ClC Chloride Channel from S. typhimurium
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 | 0015108 | molecular_function | chloride transmembrane transporter activity |
| A | 0015297 | molecular_function | antiporter activity |
| A | 0016020 | cellular_component | membrane |
| A | 0055085 | biological_process | transmembrane transport |
| A | 1902476 | biological_process | chloride transmembrane transport |
| 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 | 0015108 | molecular_function | chloride transmembrane transporter activity |
| B | 0015297 | molecular_function | antiporter activity |
| B | 0016020 | cellular_component | membrane |
| B | 0055085 | biological_process | transmembrane transport |
| B | 1902476 | biological_process | chloride transmembrane transport |
| C | 0005247 | molecular_function | voltage-gated chloride channel activity |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006811 | biological_process | monoatomic ion transport |
| C | 0006821 | biological_process | chloride transport |
| C | 0015108 | molecular_function | chloride transmembrane transporter activity |
| C | 0015297 | molecular_function | antiporter activity |
| C | 0016020 | cellular_component | membrane |
| C | 0055085 | biological_process | transmembrane transport |
| C | 1902476 | biological_process | chloride transmembrane transport |
| D | 0005247 | molecular_function | voltage-gated chloride channel activity |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006811 | biological_process | monoatomic ion transport |
| D | 0006821 | biological_process | chloride transport |
| D | 0015108 | molecular_function | chloride transmembrane transporter activity |
| D | 0015297 | molecular_function | antiporter activity |
| D | 0016020 | cellular_component | membrane |
| D | 0055085 | biological_process | transmembrane transport |
| D | 1902476 | biological_process | chloride transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 503 |
| Chain | Residue |
| A | SER107 |
| A | GLY355 |
| A | ILE356 |
| A | PHE357 |
| A | TYR445 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 504 |
| Chain | Residue |
| B | TYR445 |
| B | SER107 |
| B | GLY355 |
| B | ILE356 |
| B | PHE357 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 505 |
| Chain | Residue |
| A | ARG209 |
| B | ARG17 |
| D | MET168 |
| D | ARG169 |
| D | SER170 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 506 |
| Chain | Residue |
| A | ARG205 |
| A | ARG209 |
| A | ASN211 |
| A | LEU212 |
| A | ILE213 |
| B | ARG205 |
| B | ARG209 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 603 |
| Chain | Residue |
| C | SER107 |
| C | GLY355 |
| C | ILE356 |
| C | PHE357 |
| C | TYR445 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL D 604 |
| Chain | Residue |
| D | SER107 |
| D | GLY355 |
| D | ILE356 |
| D | PHE357 |
| D | TYR445 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 605 |
| Chain | Residue |
| B | MET168 |
| B | ARG169 |
| B | SER170 |
| C | ARG209 |
| D | ARG17 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 606 |
| Chain | Residue |
| C | ARG205 |
| C | ARG209 |
| C | ASN211 |
| C | LEU212 |
| C | ILE213 |
| D | ARG205 |
| D | ARG209 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MYS B 501 |
| Chain | Residue |
| A | ILE227 |
| B | LEU256 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MYS D 601 |
| Chain | Residue |
| C | ILE227 |
| D | LEU256 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 404 |
| Details | TOPO_DOM: Cytoplasmic |
| Chain | Residue | Details |
| A | MET1-PRO32 | |
| B | ARG167-THR176 | |
| B | GLU202-SER214 | |
| B | ARG282-GLU287 | |
| B | SER350-GLY354 | |
| B | LEU439-THR473 | |
| C | MET1-PRO32 | |
| C | GLU117-ARG123 | |
| C | ARG167-THR176 | |
| C | GLU202-SER214 | |
| C | ARG282-GLU287 | |
| A | GLU117-ARG123 | |
| C | SER350-GLY354 | |
| C | LEU439-THR473 | |
| D | MET1-PRO32 | |
| D | GLU117-ARG123 | |
| D | ARG167-THR176 | |
| D | GLU202-SER214 | |
| D | ARG282-GLU287 | |
| D | SER350-GLY354 | |
| D | LEU439-THR473 | |
| A | ARG167-THR176 | |
| A | GLU202-SER214 | |
| A | ARG282-GLU287 | |
| A | SER350-GLY354 | |
| A | LEU439-THR473 | |
| B | MET1-PRO32 | |
| B | GLU117-ARG123 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 868 |
| Details | TRANSMEM: Helical |
| Chain | Residue | Details |
| A | LEU33-VAL69 | |
| A | ILE422-PHE438 | |
| B | LEU33-VAL69 | |
| B | LEU77-PHE100 | |
| B | TRP124-ALA141 | |
| B | GLU148-PHE166 | |
| B | ILE215-PHE232 | |
| B | TRP253-GLN281 | |
| B | ILE288-ILE308 | |
| B | VAL330-SER349 | |
| B | GLY355-LEU378 | |
| A | LEU77-PHE100 | |
| B | ILE422-PHE438 | |
| C | LEU33-VAL69 | |
| C | LEU77-PHE100 | |
| C | TRP124-ALA141 | |
| C | GLU148-PHE166 | |
| C | ILE215-PHE232 | |
| C | TRP253-GLN281 | |
| C | ILE288-ILE308 | |
| C | VAL330-SER349 | |
| C | GLY355-LEU378 | |
| A | TRP124-ALA141 | |
| C | ILE422-PHE438 | |
| D | LEU33-VAL69 | |
| D | LEU77-PHE100 | |
| D | TRP124-ALA141 | |
| D | GLU148-PHE166 | |
| D | ILE215-PHE232 | |
| D | TRP253-GLN281 | |
| D | ILE288-ILE308 | |
| D | VAL330-SER349 | |
| D | GLY355-LEU378 | |
| A | GLU148-PHE166 | |
| D | ILE422-PHE438 | |
| A | ILE215-PHE232 | |
| A | TRP253-GLN281 | |
| A | ILE288-ILE308 | |
| A | VAL330-SER349 | |
| A | GLY355-LEU378 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 208 |
| Details | TOPO_DOM: Periplasmic |
| Chain | Residue | Details |
| A | GLN70-PHE76 | |
| C | ASN233-LEU252 | |
| C | GLU309-SER329 | |
| C | PHE379-ALA386 | |
| D | GLN70-PHE76 | |
| D | ASN233-LEU252 | |
| D | GLU309-SER329 | |
| D | PHE379-ALA386 | |
| A | ASN233-LEU252 | |
| A | GLU309-SER329 | |
| A | PHE379-ALA386 | |
| B | GLN70-PHE76 | |
| B | ASN233-LEU252 | |
| B | GLU309-SER329 | |
| B | PHE379-ALA386 | |
| C | GLN70-PHE76 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 208 |
| Details | INTRAMEM: Helical |
| Chain | Residue | Details |
| A | ILE109-LEU116 | |
| B | PRO405-THR416 | |
| C | ILE109-LEU116 | |
| C | LEU177-ALA189 | |
| C | PRO193-ILE201 | |
| C | GLY387-SER401 | |
| C | PRO405-THR416 | |
| D | ILE109-LEU116 | |
| D | LEU177-ALA189 | |
| D | PRO193-ILE201 | |
| D | GLY387-SER401 | |
| A | LEU177-ALA189 | |
| D | PRO405-THR416 | |
| 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_FI5 |
| Number of Residues | 32 |
| Details | INTRAMEM: Note=Loop between two helices |
| Chain | Residue | Details |
| A | PHE190-ALA192 | |
| D | PHE190-ALA192 | |
| D | VAL402-ALA404 | |
| D | ASP417-LEU421 | |
| A | VAL402-ALA404 | |
| A | ASP417-LEU421 | |
| B | PHE190-ALA192 | |
| B | VAL402-ALA404 | |
| B | ASP417-LEU421 | |
| C | PHE190-ALA192 | |
| C | VAL402-ALA404 | |
| C | ASP417-LEU421 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER107 | |
| C | ILE356 | |
| C | PHE357 | |
| C | TYR445 | |
| D | SER107 | |
| D | ILE356 | |
| D | PHE357 | |
| D | TYR445 | |
| A | ILE356 | |
| A | PHE357 | |
| A | TYR445 | |
| B | SER107 | |
| B | ILE356 | |
| B | PHE357 | |
| B | TYR445 | |
| C | SER107 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| 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 | GLU148 | |
| B | GLU148 | |
| C | GLU148 | |
| D | GLU148 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | SITE: Mediates proton transfer from the protein to the inner aqueous phase |
| Chain | Residue | Details |
| A | GLU203 | |
| B | GLU203 | |
| C | GLU203 | |
| D | GLU203 |
