6QVC
CryoEM structure of the human ClC-1 chloride channel, CBS state 1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005247 | molecular_function | voltage-gated chloride channel activity |
| A | 0005254 | molecular_function | chloride channel activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006821 | biological_process | chloride transport |
| A | 0006936 | biological_process | muscle contraction |
| A | 0016020 | cellular_component | membrane |
| A | 0019227 | biological_process | neuronal action potential propagation |
| A | 0030315 | cellular_component | T-tubule |
| A | 0034220 | biological_process | monoatomic ion transmembrane transport |
| A | 0034707 | cellular_component | chloride channel complex |
| A | 0042383 | cellular_component | sarcolemma |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0055085 | biological_process | transmembrane transport |
| A | 1902476 | biological_process | chloride transmembrane transport |
| B | 0005247 | molecular_function | voltage-gated chloride channel activity |
| B | 0005254 | molecular_function | chloride channel activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006821 | biological_process | chloride transport |
| B | 0006936 | biological_process | muscle contraction |
| B | 0016020 | cellular_component | membrane |
| B | 0019227 | biological_process | neuronal action potential propagation |
| B | 0030315 | cellular_component | T-tubule |
| B | 0034220 | biological_process | monoatomic ion transmembrane transport |
| B | 0034707 | cellular_component | chloride channel complex |
| B | 0042383 | cellular_component | sarcolemma |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0055085 | biological_process | transmembrane transport |
| B | 1902476 | biological_process | chloride transmembrane transport |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1170 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
| Chain | Residue | Details |
| B | MET1-GLY118 | |
| A | THR196-THR208 | |
| A | SER247-THR268 | |
| A | GLU291-ASN301 | |
| A | ARG377-ARG390 | |
| A | ASP579-LEU988 | |
| B | HIS180-SER183 | |
| B | THR196-THR208 | |
| B | SER247-THR268 | |
| B | GLU291-ASN301 | |
| B | ARG377-ARG390 | |
| B | ASP579-LEU988 | |
| A | MET1-GLY118 | |
| A | HIS180-SER183 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 230 |
| Details | TRANSMEM: Helical => ECO:0000305|PubMed:29809153, ECO:0000305|PubMed:31022181, ECO:0000305|PubMed:37892996, ECO:0007744|PDB:6COY, ECO:0007744|PDB:6QV6 |
| Chain | Residue | Details |
| B | ILE119-TYR150 | |
| A | LEU391-PRO408 | |
| B | LEU159-CYS179 | |
| B | TYR302-VAL321 | |
| B | LEU348-VAL376 | |
| B | LEU391-PRO408 | |
| A | ILE119-TYR150 | |
| A | LEU159-CYS179 | |
| A | TYR302-VAL321 | |
| A | LEU348-VAL376 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 182 |
| Details | TOPO_DOM: Extracellular => ECO:0000305 |
| Chain | Residue | Details |
| B | ALA151-PRO158 | |
| A | LEU427-VAL457 | |
| A | GLY499-PRO521 | |
| A | HIS555-LEU557 | |
| B | TRP322-GLU347 | |
| B | GLY409-MET414 | |
| B | LEU427-VAL457 | |
| B | GLY499-PRO521 | |
| B | HIS555-LEU557 | |
| A | ALA151-PRO158 | |
| A | TRP322-GLU347 | |
| A | GLY409-MET414 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 46 |
| Details | INTRAMEM: Note=Loop between two helices => ECO:0000305|PubMed:29809153, ECO:0000305|PubMed:31022181, ECO:0000305|PubMed:37892996, ECO:0007744|PDB:6COY, ECO:0007744|PDB:6QV6 |
| Chain | Residue | Details |
| B | PRO184-SER189 | |
| A | THR476-GLY482 | |
| A | THR539-VAL540 | |
| A | SER572-PRO575 | |
| B | SER225-GLY230 | |
| B | ALA415-LEU418 | |
| B | THR476-GLY482 | |
| B | THR539-VAL540 | |
| B | SER572-PRO575 | |
| A | PRO184-SER189 | |
| A | SER225-GLY230 | |
| A | ALA415-LEU418 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 276 |
| Details | INTRAMEM: Helical => ECO:0000305|PubMed:29809153, ECO:0000305|PubMed:31022181, ECO:0000305|PubMed:37892996, ECO:0007744|PDB:6COY, ECO:0007744|PDB:6QV6 |
| Chain | Residue | Details |
| B | GLY190-LYS195 | |
| B | SER541-ALA554 | |
| B | PRO558-GLN571 | |
| B | SER576-TYR578 | |
| A | GLY190-LYS195 | |
| A | MET209-GLY224 | |
| A | LYS231-LEU246 | |
| A | VAL269-GLY280 | |
| A | THR281-ILE290 | |
| A | MET419-THR426 | |
| A | ILE458-THR475 | |
| B | MET209-GLY224 | |
| A | GLY483-VAL498 | |
| A | GLY522-HIS538 | |
| A | SER541-ALA554 | |
| A | PRO558-GLN571 | |
| A | SER576-TYR578 | |
| B | LYS231-LEU246 | |
| B | VAL269-GLY280 | |
| B | THR281-ILE290 | |
| B | MET419-THR426 | |
| B | ILE458-THR475 | |
| B | GLY483-VAL498 | |
| B | GLY522-HIS538 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P37019 |
| Chain | Residue | Details |
| B | SER189 | |
| B | PHE484 | |
| B | TYR578 | |
| A | SER189 | |
| A | PHE484 | |
| A | TYR578 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Protopore gate => ECO:0000305|PubMed:29809153 |
| Chain | Residue | Details |
| B | GLU232 | |
| A | GLU232 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q64347 |
| Chain | Residue | Details |
| B | SER886 | |
| A | SER886 |
