7CR2
human KCNQ2 in complex with retigabine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005216 | molecular_function | monoatomic ion channel activity |
A | 0005249 | molecular_function | voltage-gated potassium channel activity |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0006813 | biological_process | potassium ion transport |
A | 0016020 | cellular_component | membrane |
A | 0055085 | biological_process | transmembrane transport |
B | 0005216 | molecular_function | monoatomic ion channel activity |
B | 0005249 | molecular_function | voltage-gated potassium channel activity |
B | 0006811 | biological_process | monoatomic ion transport |
B | 0006813 | biological_process | potassium ion transport |
B | 0016020 | cellular_component | membrane |
B | 0055085 | biological_process | transmembrane transport |
C | 0005216 | molecular_function | monoatomic ion channel activity |
C | 0005249 | molecular_function | voltage-gated potassium channel activity |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0006813 | biological_process | potassium ion transport |
C | 0016020 | cellular_component | membrane |
C | 0055085 | biological_process | transmembrane transport |
D | 0005216 | molecular_function | monoatomic ion channel activity |
D | 0005249 | molecular_function | voltage-gated potassium channel activity |
D | 0006811 | biological_process | monoatomic ion transport |
D | 0006813 | biological_process | potassium ion transport |
D | 0016020 | cellular_component | membrane |
D | 0055085 | biological_process | transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue FBX A 801 |
Chain | Residue |
A | TRP236 |
A | PHE305 |
A | PRO308 |
B | LEU299 |
B | SER303 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue FBX B 801 |
Chain | Residue |
C | SER303 |
B | TRP236 |
B | PHE305 |
B | PRO308 |
C | LEU299 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue FBX C 801 |
Chain | Residue |
C | TRP236 |
C | PHE305 |
C | PRO308 |
D | LEU299 |
D | SER303 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue FBX D 801 |
Chain | Residue |
A | LEU299 |
A | SER303 |
D | TRP236 |
D | PHE305 |
D | PRO308 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=Segment S1 => ECO:0000255 |
Chain | Residue | Details |
A | ALA92-PHE112 | |
B | ALA92-PHE112 | |
C | ALA92-PHE112 | |
D | ALA92-PHE112 |
site_id | SWS_FT_FI2 |
Number of Residues | 128 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | SER113-SER122 | |
C | GLN188-SER195 | |
C | ALA253-TYR264 | |
C | GLN286-ARG291 | |
D | SER113-SER122 | |
D | GLN188-SER195 | |
D | ALA253-TYR264 | |
D | GLN286-ARG291 | |
A | GLN188-SER195 | |
A | ALA253-TYR264 | |
A | GLN286-ARG291 | |
B | SER113-SER122 | |
B | GLN188-SER195 | |
B | ALA253-TYR264 | |
B | GLN286-ARG291 | |
C | SER113-SER122 |
site_id | SWS_FT_FI3 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=Segment S2 => ECO:0000255 |
Chain | Residue | Details |
A | GLU123-VAL143 | |
B | GLU123-VAL143 | |
C | GLU123-VAL143 | |
D | GLU123-VAL143 |
site_id | SWS_FT_FI4 |
Number of Residues | 136 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | ARG144-LYS166 | |
A | LYS219-GLU231 | |
B | ARG144-LYS166 | |
B | LYS219-GLU231 | |
C | ARG144-LYS166 | |
C | LYS219-GLU231 | |
D | ARG144-LYS166 | |
D | LYS219-GLU231 |
site_id | SWS_FT_FI5 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=Segment S3 => ECO:0000255 |
Chain | Residue | Details |
A | PRO167-SER187 | |
B | PRO167-SER187 | |
C | PRO167-SER187 | |
D | PRO167-SER187 |
site_id | SWS_FT_FI6 |
Number of Residues | 88 |
Details | TRANSMEM: Helical; Voltage-sensor; Name=Segment S4 => ECO:0000255 |
Chain | Residue | Details |
A | ALA196-TRP218 | |
B | ALA196-TRP218 | |
C | ALA196-TRP218 | |
D | ALA196-TRP218 |
site_id | SWS_FT_FI7 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=Segment S5 => ECO:0000255 |
Chain | Residue | Details |
A | LEU232-LEU252 | |
B | LEU232-LEU252 | |
C | LEU232-LEU252 | |
D | LEU232-LEU252 |
site_id | SWS_FT_FI8 |
Number of Residues | 80 |
Details | INTRAMEM: Pore-forming; Name=Segment H5 => ECO:0000255 |
Chain | Residue | Details |
A | ALA265-PRO285 | |
B | ALA265-PRO285 | |
C | ALA265-PRO285 | |
D | ALA265-PRO285 |
site_id | SWS_FT_FI9 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=Segment S6 => ECO:0000255 |
Chain | Residue | Details |
A | LEU292-LEU312 | |
B | LEU292-LEU312 | |
C | LEU292-LEU312 | |
D | LEU292-LEU312 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:16319223 |
Chain | Residue | Details |
A | THR217 | |
B | THR217 | |
C | THR217 | |
D | THR217 |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Z351 |
Chain | Residue | Details |
A | SER466 | |
B | SER478 | |
C | SER466 | |
C | SER468 | |
C | SER472 | |
C | SER476 | |
C | SER478 | |
D | SER466 | |
D | SER468 | |
D | SER472 | |
D | SER476 | |
A | SER468 | |
D | SER478 | |
A | SER472 | |
A | SER476 | |
A | SER478 | |
B | SER466 | |
B | SER468 | |
B | SER472 | |
B | SER476 |
site_id | SWS_FT_FI12 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O88943 |
Chain | Residue | Details |
A | SER507 | |
A | SER672 | |
B | SER507 | |
B | SER672 | |
C | SER507 | |
C | SER672 | |
D | SER507 | |
D | SER672 |