8HVT
Structure of the human CLC-7/Ostm1 complex reveals a novel state
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005247 | molecular_function | voltage-gated chloride channel activity |
A | 0005254 | molecular_function | chloride channel activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005764 | cellular_component | lysosome |
A | 0005765 | cellular_component | lysosomal membrane |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0006821 | biological_process | chloride transport |
A | 0015108 | molecular_function | chloride transmembrane transporter activity |
A | 0015297 | molecular_function | antiporter activity |
A | 0016020 | cellular_component | membrane |
A | 0030321 | biological_process | transepithelial chloride transport |
A | 0034707 | cellular_component | chloride channel complex |
A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
A | 0055085 | biological_process | transmembrane transport |
A | 1902476 | biological_process | chloride transmembrane transport |
C | 0005247 | molecular_function | voltage-gated chloride channel activity |
C | 0005254 | molecular_function | chloride channel activity |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005764 | cellular_component | lysosome |
C | 0005765 | cellular_component | lysosomal membrane |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0006821 | biological_process | chloride transport |
C | 0015108 | molecular_function | chloride transmembrane transporter activity |
C | 0015297 | molecular_function | antiporter activity |
C | 0016020 | cellular_component | membrane |
C | 0030321 | biological_process | transepithelial chloride transport |
C | 0034707 | cellular_component | chloride channel complex |
C | 0043231 | cellular_component | intracellular membrane-bounded organelle |
C | 0055085 | biological_process | transmembrane transport |
C | 1902476 | biological_process | chloride transmembrane transport |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 504 |
Details | TOPO_DOM: Lumenal => ECO:0000255 |
Chain | Residue | Details |
B | ALA32-PRO284 | |
D | ALA32-PRO284 | |
C | MET1-ARG126 | |
C | ILE598-THR805 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
B | VAL285-LEU305 | |
A | TYR579-PHE597 | |
C | TRP127-ILE159 | |
C | PHE174-ILE197 | |
C | ARG223-GLY241 | |
C | GLU247-GLY264 | |
C | PHE322-VAL341 | |
C | ILE375-ARG405 | |
C | PRO410-ILE432 | |
C | PRO487-LEU507 | |
C | GLY512-LEU535 | |
D | VAL285-LEU305 | |
C | TYR579-PHE597 | |
A | ARG223-GLY241 | |
A | GLU247-GLY264 | |
A | PHE322-VAL341 | |
A | ILE375-ARG405 | |
A | PRO410-ILE432 | |
A | PRO487-LEU507 | |
A | GLY512-LEU535 |
site_id | SWS_FT_FI3 |
Number of Residues | 56 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
B | HIS306-ASN334 | |
C | THR563-THR574 | |
D | HIS306-ASN334 | |
A | PRO304-LEU312 | |
A | GLY545-ILE559 | |
A | THR563-THR574 | |
C | ILE206-LEU213 | |
C | PHE288-ALA300 | |
C | PRO304-LEU312 | |
C | GLY545-ILE559 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER322 | |
D | SER322 | |
C | VAL560-MET562 | |
C | SER575-THR578 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
B | SER325 | |
C | THR783 | |
D | SER325 | |
A | TYR602 | |
A | HIS658 | |
A | THR783 | |
C | SER204 | |
C | PHE514 | |
C | TYR602 | |
C | HIS658 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
B | SER333 | |
D | SER333 |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
B | ASN93 | |
B | ASN274 | |
D | ASN93 | |
D | ASN128 | |
D | ASN135 | |
D | ASN163 | |
D | ASN177 | |
D | ASN184 | |
D | ASN194 | |
D | ASN216 | |
D | ASN263 | |
B | ASN128 | |
D | ASN274 | |
B | ASN135 | |
B | ASN163 | |
B | ASN177 | |
B | ASN184 | |
B | ASN194 | |
B | ASN216 | |
B | ASN263 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O70496 |
Chain | Residue | Details |
A | SER9 | |
C | SER9 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER60 | |
C | SER60 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER801 | |
C | SER801 |