7P5C
Cryo-EM structure of human TTYH3 in Ca2+ and GDN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005225 | molecular_function | volume-sensitive anion channel activity |
| A | 0005229 | molecular_function | intracellularly calcium-gated chloride channel activity |
| A | 0005254 | molecular_function | chloride channel activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006821 | biological_process | chloride transport |
| A | 0015813 | biological_process | L-glutamate transmembrane transport |
| A | 0016020 | cellular_component | membrane |
| A | 0034220 | biological_process | monoatomic ion transmembrane transport |
| A | 0034707 | cellular_component | chloride channel complex |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0072320 | molecular_function | volume-sensitive chloride channel activity |
| A | 1902476 | biological_process | chloride transmembrane transport |
| B | 0005225 | molecular_function | volume-sensitive anion channel activity |
| B | 0005229 | molecular_function | intracellularly calcium-gated chloride channel activity |
| B | 0005254 | molecular_function | chloride channel activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006821 | biological_process | chloride transport |
| B | 0015813 | biological_process | L-glutamate transmembrane transport |
| B | 0016020 | cellular_component | membrane |
| B | 0034220 | biological_process | monoatomic ion transmembrane transport |
| B | 0034707 | cellular_component | chloride channel complex |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0072320 | molecular_function | volume-sensitive chloride channel activity |
| B | 1902476 | biological_process | chloride transmembrane transport |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
| Chain | Residue | Details |
| A | LEU43-PHE63 | |
| B | LEU43-PHE63 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 280 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:18260827 |
| Chain | Residue | Details |
| A | TYR64-THR86 | |
| A | ARG233-LYS236 | |
| A | SER408-HIS523 | |
| B | TYR64-THR86 | |
| B | ARG233-LYS236 | |
| B | SER408-HIS523 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
| Chain | Residue | Details |
| A | ALA87-GLY107 | |
| B | ALA87-GLY107 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 462 |
| Details | TOPO_DOM: Extracellular => ECO:0000305|PubMed:18260827 |
| Chain | Residue | Details |
| A | ASN108-LEU211 | |
| A | GLY258-GLU386 | |
| B | ASN108-LEU211 | |
| B | GLY258-GLU386 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY212-ILE232 | |
| B | GLY212-ILE232 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY237-LEU257 | |
| B | GLY237-LEU257 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY387-CYS407 | |
| B | GLY387-CYS407 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q6P5F7 |
| Chain | Residue | Details |
| A | GLU110 | |
| A | ASP113 | |
| B | GLU110 | |
| B | ASP113 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | SITE: Essential for the formation of the channel-pore => ECO:0000250|UniProtKB:Q9D3A9 |
| Chain | Residue | Details |
| A | ARG161 | |
| B | ARG161 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q6P5F7 |
| Chain | Residue | Details |
| A | SER496 | |
| A | SER504 | |
| B | SER496 | |
| B | SER504 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| A | SER522 | |
| B | SER522 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:34385445 |
| Chain | Residue | Details |
| A | ASN126 | |
| B | ASN126 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:34385445 |
| Chain | Residue | Details |
| A | ASN144 | |
| B | ASN144 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18260827, ECO:0000269|PubMed:34385445, ECO:0000305|PubMed:15010458 |
| Chain | Residue | Details |
| A | ASN351 | |
| B | ASN351 |
