8DXP
Structure of LRRC8C-LRRC8A(IL125) Chimera, Class 3
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3374 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | MET1-PRO22 | |
E | PHE342-GLU803 | |
F | MET1-PRO22 | |
F | PHE342-GLU803 | |
G | MET1-PRO22 | |
G | PHE342-GLU803 | |
A | PHE342-GLU803 | |
B | MET1-PRO22 | |
B | PHE342-GLU803 | |
C | MET1-PRO22 | |
C | PHE342-GLU803 | |
D | MET1-PRO22 | |
D | PHE342-GLU803 | |
E | MET1-PRO22 |
site_id | SWS_FT_FI2 |
Number of Residues | 560 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | TRP23-CYS43 | |
C | TYR126-PHE146 | |
C | VAL267-VAL287 | |
C | PHE321-LEU341 | |
D | TRP23-CYS43 | |
D | TYR126-PHE146 | |
D | VAL267-VAL287 | |
D | PHE321-LEU341 | |
E | TRP23-CYS43 | |
E | TYR126-PHE146 | |
E | VAL267-VAL287 | |
A | TYR126-PHE146 | |
E | PHE321-LEU341 | |
F | TRP23-CYS43 | |
F | TYR126-PHE146 | |
F | VAL267-VAL287 | |
F | PHE321-LEU341 | |
G | TRP23-CYS43 | |
G | TYR126-PHE146 | |
G | VAL267-VAL287 | |
G | PHE321-LEU341 | |
A | VAL267-VAL287 | |
A | PHE321-LEU341 | |
B | TRP23-CYS43 | |
B | TYR126-PHE146 | |
B | VAL267-VAL287 | |
B | PHE321-LEU341 | |
C | TRP23-CYS43 |
site_id | SWS_FT_FI3 |
Number of Residues | 791 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | THR44-LYS125 | |
E | GLN288-SER320 | |
F | THR44-LYS125 | |
F | GLN288-SER320 | |
G | THR44-LYS125 | |
G | GLN288-SER320 | |
A | GLN288-SER320 | |
B | THR44-LYS125 | |
B | GLN288-SER320 | |
C | THR44-LYS125 | |
C | GLN288-SER320 | |
D | THR44-LYS125 | |
D | GLN288-SER320 | |
E | THR44-LYS125 |
site_id | SWS_FT_FI4 |
Number of Residues | 7 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER177 | |
B | SER176 | |
C | SER177 | |
D | SER178 | |
E | SER177 | |
F | SER178 | |
G | SER178 |
site_id | SWS_FT_FI5 |
Number of Residues | 7 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q498T9 |
Chain | Residue | Details |
A | SER177 | |
B | SER176 | |
C | SER177 | |
D | SER178 | |
E | SER177 | |
F | SER178 | |
G | SER178 |
site_id | SWS_FT_FI6 |
Number of Residues | 14 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN64 | |
E | ASN70 | |
F | ASN64 | |
F | ASN70 | |
G | ASN64 | |
G | ASN70 | |
A | ASN70 | |
B | ASN64 | |
B | ASN70 | |
C | ASN64 | |
C | ASN70 | |
D | ASN64 | |
D | ASN70 | |
E | ASN64 |
site_id | SWS_FT_FI7 |
Number of Residues | 7 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q80WG5 |
Chain | Residue | Details |
A | THR176 | |
B | THR176 | |
C | THR176 | |
D | THR177 | |
E | THR176 | |
F | THR177 | |
G | THR177 |
site_id | SWS_FT_FI8 |
Number of Residues | 7 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q80WG5 |
Chain | Residue | Details |
A | SER177 | |
B | SER176 | |
C | SER177 | |
D | SER178 | |
E | SER177 | |
F | SER178 | |
G | SER178 |