6EBM
The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alpha
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0008076 | cellular_component | voltage-gated potassium channel complex |
| B | 0016020 | cellular_component | membrane |
| B | 0051260 | biological_process | protein homooligomerization |
| B | 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 | 0008076 | cellular_component | voltage-gated potassium channel complex |
| D | 0016020 | cellular_component | membrane |
| D | 0051260 | biological_process | protein homooligomerization |
| D | 0055085 | biological_process | transmembrane transport |
| F | 0005216 | molecular_function | monoatomic ion channel activity |
| F | 0005249 | molecular_function | voltage-gated potassium channel activity |
| F | 0006811 | biological_process | monoatomic ion transport |
| F | 0006813 | biological_process | potassium ion transport |
| F | 0008076 | cellular_component | voltage-gated potassium channel complex |
| F | 0016020 | cellular_component | membrane |
| F | 0051260 | biological_process | protein homooligomerization |
| F | 0055085 | biological_process | transmembrane transport |
| H | 0005216 | molecular_function | monoatomic ion channel activity |
| H | 0005249 | molecular_function | voltage-gated potassium channel activity |
| H | 0006811 | biological_process | monoatomic ion transport |
| H | 0006813 | biological_process | potassium ion transport |
| H | 0008076 | cellular_component | voltage-gated potassium channel complex |
| H | 0016020 | cellular_component | membrane |
| H | 0051260 | biological_process | protein homooligomerization |
| H | 0055085 | biological_process | transmembrane transport |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 732 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
| Chain | Residue | Details |
| B | MET1-GLY160 | |
| H | MET1-GLY160 | |
| H | CYS244-ILE254 | |
| H | SER307-MET321 | |
| B | CYS244-ILE254 | |
| B | SER307-MET321 | |
| D | MET1-GLY160 | |
| D | CYS244-ILE254 | |
| D | SER307-MET321 | |
| F | MET1-GLY160 | |
| F | CYS244-ILE254 | |
| F | SER307-MET321 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 84 |
| Details | TRANSMEM: Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
| Chain | Residue | Details |
| B | PRO161-LEU182 | |
| D | PRO161-LEU182 | |
| F | PRO161-LEU182 | |
| H | PRO161-LEU182 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 152 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430, ECO:0000305|PubMed:12151401 |
| Chain | Residue | Details |
| B | GLU183-PRO221 | |
| D | GLU183-PRO221 | |
| F | GLU183-PRO221 | |
| H | GLU183-PRO221 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 84 |
| Details | TRANSMEM: Helical; Name=Segment S2 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
| Chain | Residue | Details |
| B | PHE222-ALA243 | |
| D | PHE222-ALA243 | |
| F | PHE222-ALA243 | |
| H | PHE222-ALA243 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 84 |
| Details | TRANSMEM: Helical; Name=Segment S5 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
| Chain | Residue | Details |
| B | ARG322-TYR343 | |
| D | ARG322-TYR343 | |
| F | ARG322-TYR343 | |
| H | ARG322-TYR343 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 76 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
| Chain | Residue | Details |
| B | PHE344-ILE357 | |
| B | PRO378-LYS384 | |
| D | PHE344-ILE357 | |
| D | PRO378-LYS384 | |
| F | PHE344-ILE357 | |
| F | PRO378-LYS384 | |
| H | PHE344-ILE357 | |
| H | PRO378-LYS384 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 44 |
| Details | INTRAMEM: Helical; Name=Pore helix => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
| Chain | Residue | Details |
| B | PRO358-THR369 | |
| D | PRO358-THR369 | |
| F | PRO358-THR369 | |
| H | PRO358-THR369 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 28 |
| Details | INTRAMEM: INTRAMEM => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
| Chain | Residue | Details |
| B | THR370-VAL377 | |
| D | THR370-VAL377 | |
| F | THR370-VAL377 | |
| H | THR370-VAL377 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 112 |
| Details | TRANSMEM: Helical; Name=Segment S6 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
| Chain | Residue | Details |
| B | ILE385-TYR413 | |
| D | ILE385-TYR413 | |
| F | ILE385-TYR413 | |
| H | ILE385-TYR413 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 324 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:12151401, ECO:0000305 |
| Chain | Residue | Details |
| B | HIS414-VAL495 | |
| D | HIS414-VAL495 | |
| F | HIS414-VAL495 | |
| H | HIS414-VAL495 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | SITE: Important for normal, slow channel gating => ECO:0000269|PubMed:17766348 |
| Chain | Residue | Details |
| B | THR252 | |
| D | THR252 | |
| F | THR252 | |
| H | THR252 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | SITE: Important for binding with the scorpion mesomartoxin; when the scorpion mesomartoxin-rKv1.2/KCNA2 interaction is modeled, this residue is close to the 'Y-57' residue of the toxin => ECO:0000305|PubMed:25514171 |
| Chain | Residue | Details |
| B | VAL377 | |
| D | VAL377 | |
| F | VAL377 | |
| H | VAL377 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P63141 |
| Chain | Residue | Details |
| B | TYR425 | |
| D | TYR425 | |
| F | TYR425 | |
| H | TYR425 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63141 |
| Chain | Residue | Details |
| B | SER430 | |
| D | SER430 | |
| F | SER430 | |
| H | SER430 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18003609, ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| B | SER436 | |
| D | SER436 | |
| F | SER436 | |
| H | SER436 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| B | SER437 | |
| B | SER464 | |
| D | SER437 | |
| D | SER464 | |
| F | SER437 | |
| F | SER464 | |
| H | SER437 | |
| H | SER464 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18003609, ECO:0000269|PubMed:21602278 |
| Chain | Residue | Details |
| B | SER445 | |
| D | SER445 | |
| F | SER445 | |
| H | SER445 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000305|PubMed:21602278 |
| Chain | Residue | Details |
| B | TYR454 | |
| D | TYR454 | |
| F | TYR454 | |
| H | TYR454 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 4 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000255 |
| Chain | Residue | Details |
| B | CYS244 | |
| D | CYS244 | |
| F | CYS244 | |
| H | CYS244 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:16770729 |
| Chain | Residue | Details |
| B | GLN207 | |
| D | GLN207 | |
| F | GLN207 | |
| H | GLN207 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 44 |
| Details | TOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P63142 |
| Chain | Residue | Details |
| B | GLU274-VAL285 | |
| D | GLU274-VAL285 | |
| F | GLU274-VAL285 | |
| H | GLU274-VAL285 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| B | ASN276 | |
| D | ASN276 | |
| F | ASN276 | |
| H | ASN276 |
