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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue GLU A 301 |
Chain | Residue |
A | TYR61 |
A | HOH434 |
A | HOH442 |
A | HOH447 |
A | PRO89 |
A | LEU90 |
A | THR91 |
A | ARG96 |
A | GLY141 |
A | SER142 |
A | THR143 |
A | GLU193 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 302 |
Chain | Residue |
A | GLU42 |
A | HIS46 |
A | HOH546 |
C | GLU166 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue ZN A 303 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue ZN A 304 |
Chain | Residue |
A | HOH407 |
A | HOH411 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue ACT A 305 |
Chain | Residue |
A | ASP216 |
A | SER217 |
B | ASP248 |
site_id | AC6 |
Number of Residues | 26 |
Details | binding site for residue 9TE B 901 |
Chain | Residue |
A | LYS104 |
A | PRO105 |
A | PHE106 |
A | MET107 |
A | SER108 |
A | SER217 |
A | LYS218 |
A | GLY219 |
A | ASN242 |
A | LEU247 |
A | HOH416 |
A | HOH470 |
A | HOH553 |
A | HOH554 |
B | LYS104 |
B | PRO105 |
B | PHE106 |
B | MET107 |
B | SER108 |
B | SER217 |
B | LYS218 |
B | GLY219 |
B | ASN242 |
B | LEU247 |
B | HOH1053 |
B | HOH1069 |
site_id | AC7 |
Number of Residues | 13 |
Details | binding site for residue GLU B 902 |
Chain | Residue |
B | TYR61 |
B | PRO89 |
B | LEU90 |
B | THR91 |
B | ARG96 |
B | LEU138 |
B | GLY141 |
B | SER142 |
B | THR143 |
B | GLU193 |
B | HOH1015 |
B | HOH1043 |
B | HOH1061 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue ZN B 903 |
Chain | Residue |
B | GLU42 |
B | LYS45 |
B | HIS46 |
B | HOH1063 |
B | HOH1140 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue ZN B 904 |
Chain | Residue |
B | ASP139 |
B | HOH1017 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue ZN B 905 |
Chain | Residue |
B | ASP156 |
B | HOH1052 |
B | HOH1124 |
B | HOH1133 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue ZN B 906 |
Chain | Residue |
B | ASP65 |
B | ACT909 |
B | HOH1122 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue ZN B 907 |
Chain | Residue |
B | HIS46 |
B | HOH1158 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue ZN B 908 |
Chain | Residue |
B | HOH1006 |
B | HOH1007 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue ACT B 909 |
Chain | Residue |
B | ASP65 |
B | ASP67 |
B | ZN906 |
B | HOH1008 |
site_id | AD6 |
Number of Residues | 18 |
Details | binding site for residue 9TE C 301 |
Chain | Residue |
C | HOH402 |
C | HOH403 |
C | LYS104 |
C | PRO105 |
C | PRO105 |
C | PHE106 |
C | PHE106 |
C | MET107 |
C | MET107 |
C | SER108 |
C | SER217 |
C | LYS218 |
C | LYS218 |
C | GLY219 |
C | ASN242 |
C | ASN242 |
C | LEU247 |
C | HOH401 |
site_id | AD7 |
Number of Residues | 12 |
Details | binding site for residue GLU C 302 |
Chain | Residue |
C | TYR61 |
C | PRO89 |
C | LEU90 |
C | THR91 |
C | ARG96 |
C | GLY141 |
C | SER142 |
C | THR143 |
C | GLU193 |
C | HOH433 |
C | HOH467 |
C | HOH484 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue ZN C 303 |
Chain | Residue |
C | HIS46 |
C | HOH510 |
C | HOH580 |
C | HOH584 |
site_id | AD9 |
Number of Residues | 3 |
Details | binding site for residue ZN C 304 |
Chain | Residue |
C | ASP156 |
C | HOH415 |
C | HOH578 |
site_id | AE1 |
Number of Residues | 3 |
Details | binding site for residue ZN C 305 |
Chain | Residue |
C | HIS23 |
C | GLU30 |
C | ACT312 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue ZN C 306 |
Chain | Residue |
C | GLU42 |
C | HIS46 |
C | LEU241 |
C | HOH422 |
site_id | AE3 |
Number of Residues | 2 |
Details | binding site for residue ZN C 307 |
Chain | Residue |
C | HOH407 |
C | HOH458 |
site_id | AE4 |
Number of Residues | 2 |
Details | binding site for residue ZN C 308 |
Chain | Residue |
C | ASP126 |
C | HOH525 |
site_id | AE5 |
Number of Residues | 1 |
Details | binding site for residue ZN C 309 |
site_id | AE6 |
Number of Residues | 2 |
Details | binding site for residue ZN C 310 |
Chain | Residue |
C | HOH404 |
C | HOH421 |
site_id | AE7 |
Number of Residues | 3 |
Details | binding site for residue ACT C 311 |
Chain | Residue |
C | ARG180 |
C | SER184 |
C | LYS187 |
site_id | AE8 |
Number of Residues | 5 |
Details | binding site for residue ACT C 312 |
Chain | Residue |
C | LYS20 |
C | HIS23 |
C | GLU30 |
C | ZN305 |
C | HOH480 |
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 | |
A | THR91 | |
A | ARG96 | |
A | SER142 | |
A | THR143 | |
A | GLU193 | |
B | PRO89 | |
B | THR91 | |
B | ARG96 | |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
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 | |
C | ARG64 | |
C | ARG148 | |
C | LYS240 | |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | SITE: Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405 |
Chain | Residue | Details |
A | ILE121 | |
B | ILE121 | |
C | ILE121 | |
Chain | Residue | Details |
A | SER150 | |
B | SER150 | |
C | SER150 | |
Chain | Residue | Details |
A | SER184 | |
B | SER184 | |
C | SER184 | |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN3 | |
B | ASN3 | |
C | ASN3 | |