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 | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16483599 |
Chain | Residue | Details |
G | TYR61 | |
H | TYR61 | |
H | ARG96 | |
H | GLU193 | |
J | TYR61 | |
J | ARG96 | |
J | GLU193 | |
L | TYR61 | |
L | ARG96 | |
L | GLU193 | |
N | TYR61 | |
G | ARG96 | |
N | ARG96 | |
N | GLU193 | |
P | TYR61 | |
P | ARG96 | |
P | GLU193 | |
G | GLU193 | |
B | TYR61 | |
B | ARG96 | |
B | GLU193 | |
E | TYR61 | |
E | ARG96 | |
E | GLU193 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
G | PRO89 | |
B | PRO89 | |
E | PRO89 | |
H | PRO89 | |
J | PRO89 | |
L | PRO89 | |
N | PRO89 | |
P | PRO89 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25103405 |
Chain | Residue | Details |
G | THR91 | |
H | THR91 | |
H | SER142 | |
H | THR143 | |
J | THR91 | |
J | SER142 | |
J | THR143 | |
L | THR91 | |
L | SER142 | |
L | THR143 | |
N | THR91 | |
G | SER142 | |
N | SER142 | |
N | THR143 | |
P | THR91 | |
P | SER142 | |
P | THR143 | |
G | THR143 | |
B | THR91 | |
B | SER142 | |
B | THR143 | |
E | THR91 | |
E | SER142 | |
E | THR143 |
site_id | SWS_FT_FI4 |
Number of Residues | 24 |
Details | SITE: Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 |
Chain | Residue | Details |
G | ARG64 | |
H | ARG64 | |
H | ARG148 | |
H | LYS240 | |
J | ARG64 | |
J | ARG148 | |
J | LYS240 | |
L | ARG64 | |
L | ARG148 | |
L | LYS240 | |
N | ARG64 | |
G | ARG148 | |
N | ARG148 | |
N | LYS240 | |
P | ARG64 | |
P | ARG148 | |
P | LYS240 | |
G | LYS240 | |
B | ARG64 | |
B | ARG148 | |
B | LYS240 | |
E | ARG64 | |
E | ARG148 | |
E | LYS240 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | SITE: Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405 |
Chain | Residue | Details |
G | ILE121 | |
B | ILE121 | |
E | ILE121 | |
H | ILE121 | |
J | ILE121 | |
L | ILE121 | |
N | ILE121 | |
P | ILE121 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8848293 |
Chain | Residue | Details |
G | SER150 | |
B | SER150 | |
E | SER150 | |
H | SER150 | |
J | SER150 | |
L | SER150 | |
N | SER150 | |
P | SER150 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine; by PKG => ECO:0000269|PubMed:8848293 |
Chain | Residue | Details |
G | SER184 | |
B | SER184 | |
E | SER184 | |
H | SER184 | |
J | SER184 | |
L | SER184 | |
N | SER184 | |
P | SER184 |