1OTT
Structure of the Escherichia coli ClC Chloride channel E148A mutant and Fab Complex
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 |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0030183 | biological_process | B cell differentiation |
| D | 0042105 | cellular_component | alpha-beta T cell receptor complex |
| F | 0005576 | cellular_component | extracellular region |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0030183 | biological_process | B cell differentiation |
| F | 0042105 | cellular_component | alpha-beta T cell receptor complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL A 466 |
| Chain | Residue |
| A | GLY146 |
| A | ARG147 |
| A | ALA148 |
| A | GLY355 |
| A | ILE356 |
| A | PHE357 |
| A | ALA358 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 467 |
| Chain | Residue |
| A | GLY355 |
| A | ILE356 |
| A | TYR445 |
| A | SER107 |
| A | GLY149 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 468 |
| Chain | Residue |
| A | GLY106 |
| A | SER107 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 466 |
| Chain | Residue |
| B | GLY146 |
| B | ARG147 |
| B | ALA148 |
| B | GLY355 |
| B | PHE357 |
| B | ALA358 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 467 |
| Chain | Residue |
| B | SER107 |
| B | GLY149 |
| B | GLY355 |
| B | ILE356 |
| B | TYR445 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 468 |
| Chain | Residue |
| B | SER107 |
| B | PRO110 |
| B | ILE448 |
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 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 194 |
| Details | Domain: {"description":"Ig-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
