4KKA
Structure of the E148A mutant of CLC-ec1 deltaNC construct in 100mM fluoride and 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 | 0015108 | molecular_function | chloride transmembrane transporter activity |
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 | 0015108 | molecular_function | chloride transmembrane transporter activity |
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 | Transmembrane: {"description":"Helical"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 106 |
Details | Topological domain: {"description":"Periplasmic"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 104 |
Details | Intramembrane: {"description":"Helical"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 64 |
Details | Topological domain: {"description":"Cytoplasmic"} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | Intramembrane: {"description":"Note=Loop between two helices"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | Motif: {"description":"Selectivity filter part_1"} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | Motif: {"description":"Selectivity filter part_2"} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | Motif: {"description":"Selectivity filter part_3"} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12649487","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16341087","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18678918","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1OTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OTU","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12649487","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OTS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ENE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6LSC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12649487","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OTT","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12649487","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OTS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OTU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ENE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6LSC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | Site: {"description":"Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport"} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | Site: {"description":"Mediates proton transfer from the protein to the inner aqueous phase"} |
Chain | Residue | Details |