8FPL
LBD conformation 2 (LBDconf2) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 10mM CaCl2, 150mM NaCl, 1mM MgCl2, 330uM CTZ, and 100uM CNQX (Closed-CaNaMg)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005216 | molecular_function | monoatomic ion channel activity |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
A | 0016020 | cellular_component | membrane |
A | 0038023 | molecular_function | signaling receptor activity |
B | 0005216 | molecular_function | monoatomic ion channel activity |
B | 0006811 | biological_process | monoatomic ion transport |
B | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
B | 0016020 | cellular_component | membrane |
B | 0038023 | molecular_function | signaling receptor activity |
C | 0005216 | molecular_function | monoatomic ion channel activity |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
C | 0016020 | cellular_component | membrane |
C | 0038023 | molecular_function | signaling receptor activity |
D | 0005216 | molecular_function | monoatomic ion channel activity |
D | 0006811 | biological_process | monoatomic ion transport |
D | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
D | 0016020 | cellular_component | membrane |
D | 0038023 | molecular_function | signaling receptor activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2780 |
Details | TOPO_DOM: Extracellular |
Chain | Residue | Details |
B | VAL1-ALA522 | |
B | THR617-ASN791 | |
C | VAL1-ALA522 | |
C | THR617-ASN791 | |
A | VAL1-ALA522 | |
A | THR617-ASN791 | |
D | VAL1-ALA522 | |
D | THR617-ASN791 |
site_id | SWS_FT_FI2 |
Number of Residues | 160 |
Details | TRANSMEM: Helical |
Chain | Residue | Details |
B | TYR523-VAL543 | |
B | LEU596-TYR616 | |
C | TYR523-VAL543 | |
C | LEU596-TYR616 | |
A | TYR523-VAL543 | |
A | LEU596-TYR616 | |
D | TYR523-VAL543 | |
D | LEU596-TYR616 |
site_id | SWS_FT_FI3 |
Number of Residues | 320 |
Details | TOPO_DOM: Cytoplasmic |
Chain | Residue | Details |
B | SER544-GLU570 | |
D | SER544-GLU570 | |
D | ASP590-SER595 | |
D | GLU813-GLY862 | |
B | ASP590-SER595 | |
B | GLU813-GLY862 | |
C | SER544-GLU570 | |
C | ASP590-SER595 | |
C | GLU813-GLY862 | |
A | SER544-GLU570 | |
A | ASP590-SER595 | |
A | GLU813-GLY862 |
site_id | SWS_FT_FI4 |
Number of Residues | 60 |
Details | INTRAMEM: Helical; Pore-forming |
Chain | Residue | Details |
B | PHE571-GLN586 | |
C | PHE571-GLN586 | |
A | PHE571-GLN586 | |
D | PHE571-GLN586 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | INTRAMEM: |
Chain | Residue | Details |
B | GLN587-CYS589 | |
C | GLN587-CYS589 | |
A | GLN587-CYS589 | |
D | GLN587-CYS589 |
site_id | SWS_FT_FI6 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=M4 |
Chain | Residue | Details |
B | VAL792-ILE812 | |
C | VAL792-ILE812 | |
A | VAL792-ILE812 | |
D | VAL792-ILE812 |
site_id | SWS_FT_FI7 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11086992, ECO:0000269|PubMed:16483599, ECO:0007744|PDB:1FTJ, ECO:0007744|PDB:2CMO |
Chain | Residue | Details |
B | PRO478 | |
C | SER654 | |
C | THR655 | |
C | GLU705 | |
A | PRO478 | |
A | THR480 | |
A | ARG485 | |
A | SER654 | |
A | THR655 | |
A | GLU705 | |
D | PRO478 | |
B | THR480 | |
D | THR480 | |
D | ARG485 | |
D | SER654 | |
D | THR655 | |
D | GLU705 | |
B | ARG485 | |
B | SER654 | |
B | THR655 | |
B | GLU705 | |
C | PRO478 | |
C | THR480 | |
C | ARG485 |
site_id | SWS_FT_FI8 |
Number of Residues | 12 |
Details | SITE: Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 |
Chain | Residue | Details |
B | ARG453 | |
D | ARG453 | |
D | ARG660 | |
D | LYS752 | |
B | ARG660 | |
B | LYS752 | |
C | ARG453 | |
C | ARG660 | |
C | LYS752 | |
A | ARG453 | |
A | ARG660 | |
A | LYS752 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | SITE: Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405 |
Chain | Residue | Details |
B | ILE633 | |
C | ILE633 | |
A | ILE633 | |
D | ILE633 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 |
Chain | Residue | Details |
B | SER662 | |
C | SER662 | |
A | SER662 | |
D | SER662 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 |
Chain | Residue | Details |
B | SER696 | |
C | SER696 | |
A | SER696 | |
D | SER696 |
site_id | SWS_FT_FI12 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P23819 |
Chain | Residue | Details |
B | SER839 | |
D | SER839 | |
D | SER842 | |
D | SER865 | |
B | SER842 | |
B | SER865 | |
C | SER839 | |
C | SER842 | |
C | SER865 | |
A | SER839 | |
A | SER842 | |
A | SER865 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15240807, ECO:0000269|PubMed:20547133 |
Chain | Residue | Details |
B | TYR861 | |
C | TYR861 | |
A | TYR861 | |
D | TYR861 |
site_id | SWS_FT_FI14 |
Number of Residues | 8 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250 |
Chain | Residue | Details |
B | CYS589 | |
B | CYS815 | |
C | CYS589 | |
C | CYS815 | |
A | CYS589 | |
A | CYS815 | |
D | CYS589 | |
D | CYS815 |
site_id | SWS_FT_FI15 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873 |
Chain | Residue | Details |
B | ASN235 | |
C | ASN235 | |
A | ASN235 | |
D | ASN235 |
site_id | SWS_FT_FI16 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19946266, ECO:0000269|PubMed:21317873, ECO:0000269|PubMed:25103405 |
Chain | Residue | Details |
B | ASN349 | |
C | ASN349 | |
A | ASN349 | |
D | ASN349 |
site_id | SWS_FT_FI17 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
B | ASN385 | |
B | ASN392 | |
C | ASN385 | |
C | ASN392 | |
A | ASN385 | |
A | ASN392 | |
D | ASN385 | |
D | ASN392 |