9B63
GluA2 flip Q in complex with TARPgamma2 at pH5, consensus structure of TMD-TARPgamma2
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2780 |
| Details | TOPO_DOM: Extracellular |
| Chain | Residue | Details |
| C | VAL1-ALA522 | |
| E | SER104-ALA124 | |
| E | ILE134-ILE154 | |
| E | PHE182-ILE202 | |
| G | MET10-THR30 | |
| G | SER104-ALA124 | |
| G | ILE134-ILE154 | |
| G | PHE182-ILE202 | |
| C | THR617-ASN791 | |
| B | VAL1-ALA522 | |
| B | THR617-ASN791 | |
| A | VAL1-ALA522 | |
| A | THR617-ASN791 | |
| D | VAL1-ALA522 | |
| D | THR617-ASN791 | |
| E | MET10-THR30 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 160 |
| Details | TRANSMEM: Helical |
| Chain | Residue | Details |
| C | TYR523-VAL543 | |
| C | LEU596-TYR616 | |
| B | TYR523-VAL543 | |
| B | 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 |
| C | SER544-GLU570 | |
| D | SER544-GLU570 | |
| D | ASP590-SER595 | |
| D | GLU813-GLY862 | |
| C | ASP590-SER595 | |
| C | GLU813-GLY862 | |
| B | SER544-GLU570 | |
| B | ASP590-SER595 | |
| B | 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 |
| C | PHE571-GLN586 | |
| B | PHE571-GLN586 | |
| A | PHE571-GLN586 | |
| D | PHE571-GLN586 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | INTRAMEM: |
| Chain | Residue | Details |
| C | GLN587-CYS589 | |
| B | 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 |
| C | VAL792-ILE812 | |
| B | 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 |
| C | PRO478 | |
| B | SER654 | |
| B | THR655 | |
| B | GLU705 | |
| A | PRO478 | |
| A | THR480 | |
| A | ARG485 | |
| A | SER654 | |
| A | THR655 | |
| A | GLU705 | |
| D | PRO478 | |
| C | THR480 | |
| D | THR480 | |
| D | ARG485 | |
| D | SER654 | |
| D | THR655 | |
| D | GLU705 | |
| C | ARG485 | |
| C | SER654 | |
| C | THR655 | |
| C | GLU705 | |
| B | PRO478 | |
| B | THR480 | |
| B | 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 |
| C | ARG453 | |
| D | ARG453 | |
| D | ARG660 | |
| D | LYS752 | |
| C | ARG660 | |
| C | LYS752 | |
| B | ARG453 | |
| B | ARG660 | |
| B | 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 |
| C | ILE633 | |
| B | 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 |
| C | SER662 | |
| B | 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 |
| C | SER696 | |
| B | 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 |
| C | SER839 | |
| D | SER839 | |
| D | SER842 | |
| D | ASN859 | |
| C | SER842 | |
| C | ASN859 | |
| B | SER839 | |
| B | SER842 | |
| B | ASN859 | |
| A | SER839 | |
| A | SER842 | |
| A | ASN859 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15240807, ECO:0000269|PubMed:20547133 |
| Chain | Residue | Details |
| C | LYS855 | |
| B | LYS855 | |
| A | LYS855 | |
| D | LYS855 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 8 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000250 |
| Chain | Residue | Details |
| C | CYS589 | |
| C | CYS815 | |
| B | CYS589 | |
| B | 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 |
| C | ASN235 | |
| B | 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 |
| C | ASN349 | |
| B | 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 |
| C | ASN385 | |
| C | ASN392 | |
| B | ASN385 | |
| B | ASN392 | |
| A | ASN385 | |
| A | ASN392 | |
| D | ASN385 | |
| D | ASN392 |
