8DRO
LRRC8A:C conformation 1 (round) LRR focus 2
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0005506 | molecular_function | iron ion binding |
B | 0009055 | molecular_function | electron transfer activity |
B | 0020037 | molecular_function | heme binding |
B | 0022900 | biological_process | electron transport chain |
B | 0042597 | cellular_component | periplasmic space |
B | 0046872 | molecular_function | metal ion binding |
C | 0005506 | molecular_function | iron ion binding |
C | 0009055 | molecular_function | electron transfer activity |
C | 0020037 | molecular_function | heme binding |
C | 0022900 | biological_process | electron transport chain |
C | 0042597 | cellular_component | periplasmic space |
C | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1220 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:29769723 |
Chain | Residue | Details |
B | MET-91-PRO-70 | |
B | TRP143-TYR264 | |
B | TRP342-ALA810 | |
C | MET-91-PRO-70 | |
C | TRP143-TYR264 | |
C | TRP342-ALA810 |
site_id | SWS_FT_FI2 |
Number of Residues | 174 |
Details | TRANSMEM: Helical => ECO:0000305|PubMed:30775971, ECO:0007744|PDB:6NZW, ECO:0007744|PDB:6NZZ, ECO:0007744|PDB:6O00 |
Chain | Residue | Details |
B | TRP-69-VAL-45 | |
B | TYR124-PHE142 | |
B | MET265-VAL286 | |
B | LEU317-TRP341 | |
C | TRP-69-VAL-45 | |
C | TYR124-PHE142 | |
C | MET265-VAL286 | |
C | LEU317-TRP341 |
site_id | SWS_FT_FI3 |
Number of Residues | 58 |
Details | TOPO_DOM: Extracellular => ECO:0000305|PubMed:29769723 |
Chain | Residue | Details |
B | HIS287-THR316 | |
C | HIS287-THR316 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Required for anion selectivity => ECO:0000250|UniProtKB:Q8IWT6 |
Chain | Residue | Details |
B | ARG103 | |
C | ARG103 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:Q8IWT6 |
Chain | Residue | Details |
B | MET-91 | |
C | MET-91 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
B | THR200 | |
C | THR200 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
B | SER202 | |
C | SER202 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q8IWT6 |
Chain | Residue | Details |
B | THR215 | |
C | THR215 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8IWT6 |
Chain | Residue | Details |
B | SER217 | |
C | SER217 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
B | ASN-26 | |
C | ASN-26 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
B | TRP-9 | |
B | ILE86 | |
C | TRP-9 | |
C | ILE86 |