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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 301 |
Chain | Residue |
A | MET107 |
A | SER108 |
A | HOH438 |
A | HOH549 |
A | HOH611 |
B | SER217 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue SO4 A 302 |
Chain | Residue |
A | HOH401 |
A | HOH402 |
A | HOH406 |
A | HOH468 |
A | HOH633 |
A | SER140 |
A | LYS144 |
A | ARG148 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 303 |
Chain | Residue |
A | ARG64 |
A | LYS69 |
A | HOH639 |
site_id | AC4 |
Number of Residues | 19 |
Details | binding site for residue 5XP A 304 |
Chain | Residue |
A | GLU13 |
A | SER14 |
A | TYR16 |
A | TYR61 |
A | PRO89 |
A | LEU90 |
A | THR91 |
A | ARG96 |
A | GLY141 |
A | SER142 |
A | THR143 |
A | LEU192 |
A | GLU193 |
A | THR195 |
A | MET196 |
A | EDO307 |
A | HOH418 |
A | HOH453 |
A | HOH574 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL A 305 |
Chain | Residue |
A | ASP248 |
A | ASN252 |
B | ASN214 |
B | ASP216 |
B | SER217 |
B | HOH576 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue ACT A 306 |
Chain | Residue |
A | ALA153 |
A | HOH506 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue EDO A 307 |
Chain | Residue |
A | GLU13 |
A | SER14 |
A | 5XP304 |
A | HOH574 |
A | HOH594 |
A | HOH706 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO A 308 |
Chain | Residue |
A | ARG148 |
A | TRP159 |
A | ARG163 |
A | HOH403 |
A | HOH637 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue EDO A 309 |
Chain | Residue |
A | LYS144 |
A | ARG163 |
A | PHE170 |
A | HOH600 |
A | HOH606 |
B | GLU24 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue EDO A 310 |
Chain | Residue |
A | HIS46 |
A | LYS240 |
A | GLN244 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue EDO A 311 |
Chain | Residue |
A | LYS116 |
A | LYS185 |
A | HOH421 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue LI A 312 |
Chain | Residue |
A | ASN242 |
A | HOH467 |
A | HOH487 |
B | SER217 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue LI B 301 |
Chain | Residue |
B | GLU97 |
B | ILE100 |
B | ASP101 |
B | HOH456 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 302 |
Chain | Residue |
B | TYR61 |
B | PRO89 |
B | THR91 |
B | ARG96 |
B | SER142 |
B | HOH401 |
B | HOH446 |
B | HOH610 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 303 |
Chain | Residue |
A | HIS23 |
B | LYS144 |
B | ARG148 |
B | ARG163 |
B | HOH410 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 304 |
Chain | Residue |
B | GLU13 |
B | SER14 |
B | HOH429 |
B | HOH437 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue GOL B 305 |
Chain | Residue |
A | TYR80 |
A | HOH470 |
B | LYS116 |
B | LYS185 |
B | HOH413 |
B | HOH575 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue ACT B 306 |
Chain | Residue |
B | ARG172 |
B | LYS240 |
B | GLN244 |
B | HIS46 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue ACT B 307 |
Chain | Residue |
B | LYS151 |
B | ILE152 |
B | ALA153 |
B | HOH616 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue ACT B 308 |
Chain | Residue |
A | HOH443 |
B | LYS20 |
B | ASN22 |
B | HOH426 |
B | HOH441 |
site_id | AE3 |
Number of Residues | 5 |
Details | binding site for residue EDO B 309 |
Chain | Residue |
B | LYS60 |
B | TYR61 |
B | GLY62 |
B | ARG96 |
B | HOH568 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue EDO B 310 |
Chain | Residue |
A | ASN214 |
A | ASP216 |
A | SER217 |
B | ASP248 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | TYR61 | |
A | ARG96 | |
A | GLU193 | |
B | TYR61 | |
B | ARG96 | |
B | GLU193 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | PRO89 | |
B | PRO89 | |
Chain | Residue | Details |
A | THR91 | |
A | SER142 | |
A | THR143 | |
B | THR91 | |
B | SER142 | |
B | THR143 | |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | SITE: Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405 |
Chain | Residue | Details |
A | ARG64 | |
A | ARG148 | |
A | LYS240 | |
B | ARG64 | |
B | ARG148 | |
B | LYS240 | |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405 |
Chain | Residue | Details |
A | ILE121 | |
B | ILE121 | |
Chain | Residue | Details |
A | SER150 | |
B | SER150 | |
Chain | Residue | Details |
A | SER184 | |
B | SER184 | |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN3 | |
B | ASN3 | |