3H06
Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| B | 0016020 | cellular_component | membrane |
| E | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| E | 0016020 | cellular_component | membrane |
| G | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| G | 0016020 | cellular_component | membrane |
| H | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| H | 0016020 | cellular_component | membrane |
| J | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| J | 0016020 | cellular_component | membrane |
| L | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| L | 0016020 | cellular_component | membrane |
| N | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| N | 0016020 | cellular_component | membrane |
| P | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| P | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE VBP G 803 |
| Chain | Residue |
| G | TYR61 |
| G | HOH264 |
| G | HOH273 |
| G | HOH274 |
| G | PRO89 |
| G | THR91 |
| G | ARG96 |
| G | LEU138 |
| G | THR143 |
| G | GLU193 |
| G | MET196 |
| G | TYR220 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE VBP B 807 |
| Chain | Residue |
| B | TYR61 |
| B | PRO89 |
| B | LEU90 |
| B | THR91 |
| B | ARG96 |
| B | LEU138 |
| B | THR143 |
| B | THR174 |
| B | LEU192 |
| B | GLU193 |
| B | TYR220 |
| B | HOH296 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE VBP E 808 |
| Chain | Residue |
| E | TYR16 |
| E | TYR61 |
| E | PRO89 |
| E | LEU90 |
| E | THR91 |
| E | ARG96 |
| E | LEU138 |
| E | THR143 |
| E | THR174 |
| E | TYR190 |
| E | GLU193 |
| E | MET196 |
| E | TYR220 |
| E | HOH279 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE VBP H 806 |
| Chain | Residue |
| H | GLU13 |
| H | TYR16 |
| H | TYR61 |
| H | PRO89 |
| H | THR91 |
| H | ARG96 |
| H | LEU138 |
| H | THR143 |
| H | THR174 |
| H | GLU193 |
| H | MET196 |
| H | TYR220 |
| H | HOH279 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE VBP J 804 |
| Chain | Residue |
| J | HOH3 |
| J | TYR61 |
| J | PRO89 |
| J | LEU90 |
| J | THR91 |
| J | ARG96 |
| J | LEU138 |
| J | THR143 |
| J | LEU192 |
| J | GLU193 |
| J | MET196 |
| J | HOH273 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE VBP L 801 |
| Chain | Residue |
| L | TYR16 |
| L | TYR61 |
| L | PRO89 |
| L | LEU90 |
| L | THR91 |
| L | ARG96 |
| L | LEU138 |
| L | THR143 |
| L | THR174 |
| L | TYR190 |
| L | LEU192 |
| L | GLU193 |
| L | MET196 |
| L | TYR220 |
| L | HOH262 |
| L | HOH265 |
| L | HOH287 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE VBP N 802 |
| Chain | Residue |
| N | GLU13 |
| N | TYR61 |
| N | PRO89 |
| N | THR91 |
| N | ARG96 |
| N | THR143 |
| N | THR174 |
| N | LEU192 |
| N | GLU193 |
| N | MET196 |
| N | TYR220 |
| N | HOH266 |
| N | HOH273 |
| N | HOH292 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE VBP P 805 |
| Chain | Residue |
| P | LEU138 |
| P | THR143 |
| P | THR174 |
| P | TYR190 |
| P | LEU191 |
| P | LEU192 |
| P | GLU193 |
| P | MET196 |
| P | HOH270 |
| P | TYR61 |
| P | PRO89 |
| P | LEU90 |
| P | THR91 |
| P | ARG96 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11086992","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16483599","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FTJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CMO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Site: {"description":"Interaction with the cone snail toxin Con-ikot-ikot","evidences":[{"source":"PubMed","id":"25103405","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Site: {"description":"Crucial to convey clamshell closure to channel opening","evidences":[{"source":"PubMed","id":"25103405","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphoserine; by PKG","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






