8DRN
LRRC8A:C conformation 1 (round) LRR focus 1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005506 | molecular_function | iron ion binding |
A | 0009055 | molecular_function | electron transfer activity |
A | 0020037 | molecular_function | heme binding |
A | 0022900 | biological_process | electron transport chain |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
F | 0005225 | molecular_function | volume-sensitive anion channel activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0005783 | cellular_component | endoplasmic reticulum |
F | 0005789 | cellular_component | endoplasmic reticulum membrane |
F | 0005886 | cellular_component | plasma membrane |
F | 0015734 | biological_process | taurine transmembrane transport |
F | 0015810 | biological_process | aspartate transmembrane transport |
F | 0034214 | biological_process | protein hexamerization |
F | 0034220 | biological_process | monoatomic ion transmembrane transport |
F | 0034702 | cellular_component | monoatomic ion channel complex |
F | 0045444 | biological_process | fat cell differentiation |
F | 0055085 | biological_process | transmembrane transport |
F | 0071470 | biological_process | cellular response to osmotic stress |
F | 0098656 | biological_process | monoatomic anion transmembrane transport |
F | 0140361 | biological_process | cyclic-GMP-AMP transmembrane import across plasma membrane |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 610 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:29769723 |
Chain | Residue | Details |
A | MET-91-PRO-70 | |
A | TRP143-TYR264 | |
A | TRP342-ALA810 |
site_id | SWS_FT_FI2 |
Number of Residues | 87 |
Details | TRANSMEM: Helical => ECO:0000305|PubMed:30775971, ECO:0007744|PDB:6NZW, ECO:0007744|PDB:6NZZ, ECO:0007744|PDB:6O00 |
Chain | Residue | Details |
A | TRP-69-VAL-45 | |
A | TYR124-PHE142 | |
A | MET265-VAL286 | |
A | LEU317-TRP341 |
site_id | SWS_FT_FI3 |
Number of Residues | 29 |
Details | TOPO_DOM: Extracellular => ECO:0000305|PubMed:29769723 |
Chain | Residue | Details |
A | HIS287-THR316 | |
F | GLN288-SER320 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Required for anion selectivity => ECO:0000250|UniProtKB:Q8IWT6 |
Chain | Residue | Details |
A | ARG103 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:Q8IWT6 |
Chain | Residue | Details |
A | MET-91 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
A | THR200 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
A | SER202 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q8IWT6 |
Chain | Residue | Details |
A | THR215 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8IWT6 |
Chain | Residue | Details |
A | SER217 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN-26 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | TRP-9 | |
A | ILE86 |