Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
A | 0016020 | cellular_component | membrane |
B | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
B | 0016020 | cellular_component | membrane |
C | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
C | 0016020 | cellular_component | membrane |
D | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
D | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 264 |
Chain | Residue |
B | LYS144 |
B | ARG148 |
B | ARG163 |
B | HOH377 |
D | HIS23 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 264 |
Chain | Residue |
C | HOH418 |
C | HIS23 |
C | LYS144 |
C | ARG148 |
C | ARG163 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 264 |
Chain | Residue |
B | HIS23 |
D | LYS144 |
D | ARG148 |
D | ARG163 |
D | HOH424 |
D | HOH464 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 265 |
Chain | Residue |
C | LEU138 |
C | THR174 |
C | AT1266 |
C | HOH412 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT D 265 |
Chain | Residue |
D | THR174 |
D | HOH476 |
D | HOH477 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE AT1 A 264 |
Chain | Residue |
A | GLU13 |
A | TYR61 |
A | PRO89 |
A | LEU90 |
A | THR91 |
A | ARG96 |
A | LEU138 |
A | GLY141 |
A | SER142 |
A | THR143 |
A | GLU193 |
A | TYR220 |
A | HOH271 |
A | HOH289 |
A | HOH356 |
A | HOH374 |
A | HOH385 |
A | HOH391 |
A | HOH445 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE AT1 B 265 |
Chain | Residue |
B | GLU13 |
B | TYR61 |
B | PRO89 |
B | LEU90 |
B | THR91 |
B | ARG96 |
B | GLY141 |
B | SER142 |
B | THR143 |
B | GLU193 |
B | THR195 |
B | TYR220 |
B | HOH267 |
B | HOH294 |
B | HOH306 |
B | HOH380 |
B | HOH384 |
B | HOH446 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AT1 C 266 |
Chain | Residue |
C | GLU13 |
C | TYR61 |
C | PRO89 |
C | LEU90 |
C | THR91 |
C | ARG96 |
C | LEU138 |
C | SER142 |
C | THR143 |
C | GLU193 |
C | TYR220 |
C | SO4265 |
C | HOH270 |
C | HOH276 |
C | HOH385 |
C | HOH471 |
site_id | AC9 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE AT1 D 266 |
Chain | Residue |
D | GLU13 |
D | TYR61 |
D | PRO89 |
D | LEU90 |
D | THR91 |
D | ARG96 |
D | LEU138 |
D | GLY141 |
D | SER142 |
D | THR143 |
D | GLU193 |
D | TYR220 |
D | HOH273 |
D | HOH295 |
D | HOH308 |
D | HOH335 |
D | HOH341 |
D | HOH495 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | PRO89 | |
B | SER142 | |
B | THR143 | |
B | GLU193 | |
C | PRO89 | |
C | THR91 | |
C | ARG96 | |
C | SER142 | |
C | THR143 | |
C | GLU193 | |
D | PRO89 | |
A | THR91 | |
D | THR91 | |
D | ARG96 | |
D | SER142 | |
D | THR143 | |
D | GLU193 | |
A | ARG96 | |
A | SER142 | |
A | THR143 | |
A | GLU193 | |
B | PRO89 | |
B | THR91 | |
B | ARG96 | |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | SITE: Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 |
Chain | Residue | Details |
A | ARG64 | |
D | ARG64 | |
D | ARG148 | |
D | LYS240 | |
A | ARG148 | |
A | LYS240 | |
B | ARG64 | |
B | ARG148 | |
B | LYS240 | |
C | ARG64 | |
C | ARG148 | |
C | LYS240 | |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405 |
Chain | Residue | Details |
A | ILE121 | |
B | ILE121 | |
C | ILE121 | |
D | ILE121 | |
Chain | Residue | Details |
A | SER150 | |
B | SER150 | |
C | SER150 | |
D | SER150 | |
Chain | Residue | Details |
A | SER184 | |
B | SER184 | |
C | SER184 | |
D | SER184 | |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN3 | |
B | ASN3 | |
C | ASN3 | |
D | ASN3 | |