7SQH
Structure of the human proton-activated chloride channel ASOR in desensitized conformation
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005254 | molecular_function | chloride channel activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006821 | biological_process | chloride transport |
| A | 0009986 | cellular_component | cell surface |
| A | 0034220 | biological_process | monoatomic ion transmembrane transport |
| A | 0034707 | cellular_component | chloride channel complex |
| A | 0061797 | molecular_function | pH-gated chloride channel activity |
| A | 1902476 | biological_process | chloride transmembrane transport |
| B | 0005254 | molecular_function | chloride channel activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006821 | biological_process | chloride transport |
| B | 0009986 | cellular_component | cell surface |
| B | 0034220 | biological_process | monoatomic ion transmembrane transport |
| B | 0034707 | cellular_component | chloride channel complex |
| B | 0061797 | molecular_function | pH-gated chloride channel activity |
| B | 1902476 | biological_process | chloride transmembrane transport |
| C | 0005254 | molecular_function | chloride channel activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006821 | biological_process | chloride transport |
| C | 0009986 | cellular_component | cell surface |
| C | 0034220 | biological_process | monoatomic ion transmembrane transport |
| C | 0034707 | cellular_component | chloride channel complex |
| C | 0061797 | molecular_function | pH-gated chloride channel activity |
| C | 1902476 | biological_process | chloride transmembrane transport |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 282 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:31023925, ECO:0000305|PubMed:31318332 |
| Chain | Residue | Details |
| A | MET1-ASN64 | |
| A | LYS319-SER350 | |
| B | MET1-ASN64 | |
| B | LYS319-SER350 | |
| C | MET1-ASN64 | |
| C | LYS319-SER350 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 108 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| A | VAL65-VAL85 | |
| A | ASN302-PHE318 | |
| B | VAL65-VAL85 | |
| B | ASN302-PHE318 | |
| C | VAL65-VAL85 | |
| C | ASN302-PHE318 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 645 |
| Details | TOPO_DOM: Extracellular => ECO:0000255 |
| Chain | Residue | Details |
| A | TYR86-ALA301 | |
| B | TYR86-ALA301 | |
| C | TYR86-ALA301 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | SER9 | |
| B | SER9 | |
| C | SER9 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9D771 |
| Chain | Residue | Details |
| A | TYR10 | |
| B | TYR10 | |
| C | TYR10 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9D771 |
| Chain | Residue | Details |
| A | SER14 | |
| B | SER14 | |
| C | SER14 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q66H28 |
| Chain | Residue | Details |
| A | SER24 | |
| B | SER24 | |
| C | SER24 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973 |
| Chain | Residue | Details |
| A | ASN155 | |
| A | ASN162 | |
| B | ASN155 | |
| B | ASN162 | |
| C | ASN155 | |
| C | ASN162 |
