6UKN
Cryo-EM structure of the potassium-chloride cotransporter KCC4 in lipid nanodiscs
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006813 | biological_process | potassium ion transport |
| A | 0006884 | biological_process | cell volume homeostasis |
| A | 0007268 | biological_process | chemical synaptic transmission |
| A | 0015293 | molecular_function | symporter activity |
| A | 0015377 | molecular_function | chloride:monoatomic cation symporter activity |
| A | 0015379 | molecular_function | potassium:chloride symporter activity |
| A | 0016020 | cellular_component | membrane |
| A | 0019901 | molecular_function | protein kinase binding |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0045202 | cellular_component | synapse |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0055064 | biological_process | chloride ion homeostasis |
| A | 0055075 | biological_process | potassium ion homeostasis |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0071333 | biological_process | cellular response to glucose stimulus |
| A | 0071805 | biological_process | potassium ion transmembrane transport |
| A | 1902476 | biological_process | chloride transmembrane transport |
| A | 1990573 | biological_process | potassium ion import across plasma membrane |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Discontinuously helical; Name=1","evidences":[{"source":"UniProtKB","id":"Q9Y666","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 177 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"UniProtKB","id":"Q9Y666","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 67 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"UniProtKB","id":"Q9Y666","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"UniProtKB","id":"Q9Y666","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"UniProtKB","id":"Q9Y666","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"UniProtKB","id":"Q9Y666","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"UniProtKB","id":"Q9Y666","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"UniProtKB","id":"Q9Y666","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"UniProtKB","id":"Q9Y666","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"source":"UniProtKB","id":"Q9Y666","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=11","evidences":[{"source":"UniProtKB","id":"Q9Y666","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 15 |
| Details | Transmembrane: {"description":"Helical; Name=12","evidences":[{"source":"UniProtKB","id":"Q9Y666","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9Y666","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"23376777","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19656770","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23376777","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"23376777","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
