8F77
LRRC8A(T48D):C conformation 2 top focus
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 |
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 |
D | 0005506 | molecular_function | iron ion binding |
D | 0009055 | molecular_function | electron transfer activity |
D | 0020037 | molecular_function | heme binding |
D | 0022900 | biological_process | electron transport chain |
D | 0042597 | cellular_component | periplasmic space |
D | 0046872 | molecular_function | metal ion binding |
E | 0005506 | molecular_function | iron ion binding |
E | 0009055 | molecular_function | electron transfer activity |
E | 0020037 | molecular_function | heme binding |
E | 0022900 | biological_process | electron transport chain |
E | 0042597 | cellular_component | periplasmic space |
E | 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 | 601 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
F | MET1-PRO22 | |
F | LYS147-THR266 | |
F | PHE342-ASP803 | |
B | MET1-PRO22 | |
B | TRP143-TYR264 | |
B | TRP342-ALA810 | |
C | MET1-PRO22 | |
C | TRP143-TYR264 | |
C | TRP342-ALA810 | |
D | MET1-PRO22 | |
D | TRP143-TYR264 | |
D | TRP342-ALA810 | |
E | MET1-PRO22 | |
E | TRP143-TYR264 | |
E | TRP342-ALA810 |
site_id | SWS_FT_FI2 |
Number of Residues | 80 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
F | TRP23-CYS43 | |
F | TYR126-PHE146 | |
F | VAL267-VAL287 | |
F | PHE321-LEU341 | |
B | TRP23-VAL47 | |
B | TYR124-PHE142 | |
B | MET265-VAL286 | |
B | LEU317-TRP341 | |
C | TRP23-VAL47 | |
C | TYR124-PHE142 | |
C | MET265-VAL286 | |
C | LEU317-TRP341 | |
D | TRP23-VAL47 | |
D | TYR124-PHE142 | |
D | MET265-VAL286 | |
D | LEU317-TRP341 | |
E | TRP23-VAL47 | |
E | TYR124-PHE142 | |
E | MET265-VAL286 | |
E | LEU317-TRP341 |
site_id | SWS_FT_FI3 |
Number of Residues | 113 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
F | THR44-LYS125 | |
F | GLN288-SER320 | |
C | HIS287-THR316 | |
D | HIS287-THR316 | |
E | HIS287-THR316 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8TDW0 |
Chain | Residue | Details |
F | SER212 | |
B | ARG103 | |
C | ARG103 | |
D | ARG103 | |
E | ARG103 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q498T9 |
Chain | Residue | Details |
F | SER215 | |
B | MET1 | |
C | MET1 | |
D | MET1 | |
E | MET1 |
site_id | SWS_FT_FI6 |
Number of Residues | 5 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
A | THR200 | |
B | THR200 | |
C | THR200 | |
D | THR200 | |
E | THR200 |
site_id | SWS_FT_FI7 |
Number of Residues | 5 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
A | SER202 | |
B | SER202 | |
C | SER202 | |
D | SER202 | |
E | SER202 |
site_id | SWS_FT_FI8 |
Number of Residues | 5 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q8IWT6 |
Chain | Residue | Details |
A | THR215 | |
B | THR215 | |
C | THR215 | |
D | THR215 | |
E | THR215 |
site_id | SWS_FT_FI9 |
Number of Residues | 5 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8IWT6 |
Chain | Residue | Details |
A | SER217 | |
B | SER217 | |
C | SER217 | |
D | SER217 | |
E | SER217 |
site_id | SWS_FT_FI10 |
Number of Residues | 5 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN66 | |
B | ASN66 | |
C | ASN66 | |
D | ASN66 | |
E | ASN66 |
site_id | SWS_FT_FI11 |
Number of Residues | 10 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | TRP68 | |
A | ILE72 | |
B | TRP68 | |
B | ILE72 | |
C | TRP68 | |
C | ILE72 | |
D | TRP68 | |
D | ILE72 | |
E | TRP68 | |
E | ILE72 |