6WBL
Cryo-EM structure of human Pannexin 1 channel with deletion of N-terminal helix and C-terminal tail, in complex with CBX
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006812 | biological_process | monoatomic cation transport |
A | 0015267 | molecular_function | channel activity |
A | 0032732 | biological_process | positive regulation of interleukin-1 production |
B | 0006812 | biological_process | monoatomic cation transport |
B | 0015267 | molecular_function | channel activity |
B | 0032732 | biological_process | positive regulation of interleukin-1 production |
C | 0006812 | biological_process | monoatomic cation transport |
C | 0015267 | molecular_function | channel activity |
C | 0032732 | biological_process | positive regulation of interleukin-1 production |
D | 0006812 | biological_process | monoatomic cation transport |
D | 0015267 | molecular_function | channel activity |
D | 0032732 | biological_process | positive regulation of interleukin-1 production |
E | 0006812 | biological_process | monoatomic cation transport |
E | 0015267 | molecular_function | channel activity |
E | 0032732 | biological_process | positive regulation of interleukin-1 production |
F | 0006812 | biological_process | monoatomic cation transport |
F | 0015267 | molecular_function | channel activity |
F | 0032732 | biological_process | positive regulation of interleukin-1 production |
G | 0006812 | biological_process | monoatomic cation transport |
G | 0015267 | molecular_function | channel activity |
G | 0032732 | biological_process | positive regulation of interleukin-1 production |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 896 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | MET1-CYS40 | |
E | ARG128-ARG217 | |
F | MET1-CYS40 | |
F | ARG128-ARG217 | |
G | MET1-CYS40 | |
G | ARG128-ARG217 | |
A | ARG128-ARG217 | |
B | MET1-CYS40 | |
B | ARG128-ARG217 | |
C | MET1-CYS40 | |
C | ARG128-ARG217 | |
D | MET1-CYS40 | |
D | ARG128-ARG217 | |
E | MET1-CYS40 |
site_id | SWS_FT_FI2 |
Number of Residues | 560 |
Details | TRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU00351 |
Chain | Residue | Details |
A | ILE41-GLY61 | |
C | LYS107-TRP127 | |
C | LEU218-SER238 | |
C | LEU267-LEU287 | |
D | ILE41-GLY61 | |
D | LYS107-TRP127 | |
D | LEU218-SER238 | |
D | LEU267-LEU287 | |
E | ILE41-GLY61 | |
E | LYS107-TRP127 | |
E | LEU218-SER238 | |
A | LYS107-TRP127 | |
E | LEU267-LEU287 | |
F | ILE41-GLY61 | |
F | LYS107-TRP127 | |
F | LEU218-SER238 | |
F | LEU267-LEU287 | |
G | ILE41-GLY61 | |
G | LYS107-TRP127 | |
G | LEU218-SER238 | |
G | LEU267-LEU287 | |
A | LEU218-SER238 | |
A | LEU267-LEU287 | |
B | ILE41-GLY61 | |
B | LYS107-TRP127 | |
B | LEU218-SER238 | |
B | LEU267-LEU287 | |
C | ILE41-GLY61 |
site_id | SWS_FT_FI3 |
Number of Residues | 497 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | THR62-HIS106 | |
E | SER239-LYS266 | |
F | THR62-HIS106 | |
F | SER239-LYS266 | |
G | THR62-HIS106 | |
G | SER239-LYS266 | |
A | SER239-LYS266 | |
B | THR62-HIS106 | |
B | SER239-LYS266 | |
C | THR62-HIS106 | |
C | SER239-LYS266 | |
D | THR62-HIS106 | |
D | SER239-LYS266 | |
E | THR62-HIS106 |
site_id | SWS_FT_FI4 |
Number of Residues | 14 |
Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q9JIP4 |
Chain | Residue | Details |
A | CYS40 | |
E | CYS347 | |
F | CYS40 | |
F | CYS347 | |
G | CYS40 | |
G | CYS347 | |
A | CYS347 | |
B | CYS40 | |
B | CYS347 | |
C | CYS40 | |
C | CYS347 | |
D | CYS40 | |
D | CYS347 | |
E | CYS40 |
site_id | SWS_FT_FI5 |
Number of Residues | 7 |
Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:30814251 |
Chain | Residue | Details |
A | TYR199 | |
B | TYR199 | |
C | TYR199 | |
D | TYR199 | |
E | TYR199 | |
F | TYR199 | |
G | TYR199 |
site_id | SWS_FT_FI6 |
Number of Residues | 7 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17715132, ECO:0000269|PubMed:30918116, ECO:0000269|PubMed:32494015, ECO:0000269|PubMed:33947837 |
Chain | Residue | Details |
A | ASN255 | |
B | ASN255 | |
C | ASN255 | |
D | ASN255 | |
E | ASN255 | |
F | ASN255 | |
G | ASN255 |