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 | 405 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
A | MET1-ASN20 | |
E | ASN72-MET98 | |
F | MET1-ASN20 | |
F | ASN72-MET98 | |
G | MET1-ASN20 | |
G | ASN72-MET98 | |
H | MET1-ASN20 | |
H | ASN72-MET98 | |
I | MET1-ASN20 | |
I | ASN72-MET98 | |
A | ASN72-MET98 | |
B | MET1-ASN20 | |
B | ASN72-MET98 | |
C | MET1-ASN20 | |
C | ASN72-MET98 | |
D | MET1-ASN20 | |
D | ASN72-MET98 | |
E | MET1-ASN20 |
site_id | SWS_FT_FI2 |
Number of Residues | 135 |
Details | TRANSMEM: Helical; Name=S1 => ECO:0000269|PubMed:32832629, ECO:0007744|PDB:6LMT |
Chain | Residue | Details |
A | GLY21-SER36 | |
B | GLY21-SER36 | |
C | GLY21-SER36 | |
D | GLY21-SER36 | |
E | GLY21-SER36 | |
F | GLY21-SER36 | |
G | GLY21-SER36 | |
H | GLY21-SER36 | |
I | GLY21-SER36 |
site_id | SWS_FT_FI3 |
Number of Residues | 567 |
Details | TOPO_DOM: Extracellular => ECO:0000305 |
Chain | Residue | Details |
A | PHE37-ASN48 | |
E | LEU125-ILE177 | |
F | PHE37-ASN48 | |
F | LEU125-ILE177 | |
G | PHE37-ASN48 | |
G | LEU125-ILE177 | |
H | PHE37-ASN48 | |
H | LEU125-ILE177 | |
I | PHE37-ASN48 | |
I | LEU125-ILE177 | |
A | LEU125-ILE177 | |
B | PHE37-ASN48 | |
B | LEU125-ILE177 | |
C | PHE37-ASN48 | |
C | LEU125-ILE177 | |
D | PHE37-ASN48 | |
D | LEU125-ILE177 | |
E | PHE37-ASN48 |
site_id | SWS_FT_FI4 |
Number of Residues | 198 |
Details | TRANSMEM: Helical; Name=S2 => ECO:0000269|PubMed:32832629, ECO:0007744|PDB:6LMT |
Chain | Residue | Details |
A | TYR49-ASN71 | |
B | TYR49-ASN71 | |
C | TYR49-ASN71 | |
D | TYR49-ASN71 | |
E | TYR49-ASN71 | |
F | TYR49-ASN71 | |
G | TYR49-ASN71 | |
H | TYR49-ASN71 | |
I | TYR49-ASN71 |
site_id | SWS_FT_FI5 |
Number of Residues | 225 |
Details | TRANSMEM: Helical; Name=S3 => ECO:0000269|PubMed:32832629, ECO:0007744|PDB:6LMT |
Chain | Residue | Details |
A | LEU99-PHE124 | |
B | LEU99-PHE124 | |
C | LEU99-PHE124 | |
D | LEU99-PHE124 | |
E | LEU99-PHE124 | |
F | LEU99-PHE124 | |
G | LEU99-PHE124 | |
H | LEU99-PHE124 | |
I | LEU99-PHE124 |
site_id | SWS_FT_FI6 |
Number of Residues | 225 |
Details | TRANSMEM: Helical; Name=S4 => ECO:0000269|PubMed:32832629, ECO:0007744|PDB:6LMT |
Chain | Residue | Details |
A | LYS178-ARG203 | |
B | LYS178-ARG203 | |
C | LYS178-ARG203 | |
D | LYS178-ARG203 | |
E | LYS178-ARG203 | |
F | LYS178-ARG203 | |
G | LYS178-ARG203 | |
H | LYS178-ARG203 | |
I | LYS178-ARG203 |
site_id | SWS_FT_FI7 |
Number of Residues | 18 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:D3Z291 |
Chain | Residue | Details |
A | CYS100 | |
E | CYS205 | |
F | CYS100 | |
F | CYS205 | |
G | CYS100 | |
G | CYS205 | |
H | CYS100 | |
H | CYS205 | |
I | CYS100 | |
I | CYS205 | |
A | CYS205 | |
B | CYS100 | |
B | CYS205 | |
C | CYS100 | |
C | CYS205 | |
D | CYS100 | |
D | CYS205 | |
E | CYS100 |
site_id | SWS_FT_FI8 |
Number of Residues | 9 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:Q8IU99 |
Chain | Residue | Details |
A | ASN139 | |
B | ASN139 | |
C | ASN139 | |
D | ASN139 | |
E | ASN139 | |
F | ASN139 | |
G | ASN139 | |
H | ASN139 | |
I | ASN139 |