6LMX
Cryo-EM structure of the CALHM chimeric construct (9-mer)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005227 | molecular_function | calcium activated cation channel activity |
| A | 0005244 | molecular_function | voltage-gated ion channel activity |
| A | 0006812 | biological_process | cation transport |
| B | 0005227 | molecular_function | calcium activated cation channel activity |
| B | 0005244 | molecular_function | voltage-gated ion channel activity |
| B | 0006812 | biological_process | cation transport |
| C | 0005227 | molecular_function | calcium activated cation channel activity |
| C | 0005244 | molecular_function | voltage-gated ion channel activity |
| C | 0006812 | biological_process | cation transport |
| D | 0005227 | molecular_function | calcium activated cation channel activity |
| D | 0005244 | molecular_function | voltage-gated ion channel activity |
| D | 0006812 | biological_process | cation transport |
| E | 0005227 | molecular_function | calcium activated cation channel activity |
| E | 0005244 | molecular_function | voltage-gated ion channel activity |
| E | 0006812 | biological_process | cation transport |
| F | 0005227 | molecular_function | calcium activated cation channel activity |
| F | 0005244 | molecular_function | voltage-gated ion channel activity |
| F | 0006812 | biological_process | cation transport |
| G | 0005227 | molecular_function | calcium activated cation channel activity |
| G | 0005244 | molecular_function | voltage-gated ion channel activity |
| G | 0006812 | biological_process | cation transport |
| H | 0005227 | molecular_function | calcium activated cation channel activity |
| H | 0005244 | molecular_function | voltage-gated ion channel activity |
| H | 0006812 | biological_process | cation transport |
| I | 0005227 | molecular_function | calcium activated cation channel activity |
| I | 0005244 | molecular_function | voltage-gated ion channel activity |
| I | 0006812 | biological_process | cation transport |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 135 |
| Details | Transmembrane: {"description":"Helical; Name=S1","evidences":[{"source":"PubMed","id":"32832629","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LMT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 639 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 198 |
| Details | Transmembrane: {"description":"Helical; Name=S2","evidences":[{"source":"PubMed","id":"32832629","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LMT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 234 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 225 |
| Details | Transmembrane: {"description":"Helical; Name=S3","evidences":[{"source":"PubMed","id":"32832629","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LMT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 225 |
| Details | Transmembrane: {"description":"Helical; Name=S4","evidences":[{"source":"PubMed","id":"32832629","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LMT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 261 |
| Details | Region: {"description":"Phospholipid-binding","evidences":[{"source":"UniProtKB","id":"Q8IU99","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 18 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"D3Z291","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 9 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"UniProtKB","id":"Q8IU99","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 207 |
| Details | Transmembrane: {"description":"Helical; Name=S2","evidences":[{"source":"PubMed","id":"31776515","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6UIV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 270 |
| Details | Transmembrane: {"description":"Helical; Name=S3","evidences":[{"source":"PubMed","id":"31776515","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6UIV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 234 |
| Details | Transmembrane: {"description":"Helical; Name=S4","evidences":[{"source":"PubMed","id":"31776515","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6UIV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 333 |
| Details | Region: {"description":"Intersubunit interaction","evidences":[{"source":"PubMed","id":"31776515","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6UIV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 9 |
| Details | Site: {"description":"Not N-glycosylated","evidences":[{"source":"PubMed","id":"31776515","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
