8SDA
CryoEM structure of rat Kv2.1(1-598) L403A mutant in nanodiscs
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 | 0008076 | cellular_component | voltage-gated potassium channel complex |
| A | 0016020 | cellular_component | membrane |
| A | 0051260 | biological_process | protein homooligomerization |
| 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 | 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 |
| 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 | 0008076 | cellular_component | voltage-gated potassium channel complex |
| C | 0016020 | cellular_component | membrane |
| C | 0051260 | biological_process | protein homooligomerization |
| 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 | 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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 84 |
| Details | TRANSMEM: Helical; Name=Segment S1 => ECO:0000255 |
| Chain | Residue | Details |
| A | ALA183-LEU204 | |
| B | ALA183-LEU204 | |
| D | ALA183-LEU204 | |
| C | ALA183-LEU204 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 200 |
| Details | TOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P63142 |
| Chain | Residue | Details |
| A | ASN205-GLN224 | |
| D | GLU277-ARG290 | |
| D | ALA348-ILE360 | |
| D | PRO381-LYS387 | |
| C | ASN205-GLN224 | |
| C | GLU277-ARG290 | |
| C | ALA348-ILE360 | |
| C | PRO381-LYS387 | |
| A | GLU277-ARG290 | |
| A | ALA348-ILE360 | |
| A | PRO381-LYS387 | |
| B | ASN205-GLN224 | |
| B | GLU277-ARG290 | |
| B | ALA348-ILE360 | |
| B | PRO381-LYS387 | |
| D | ASN205-GLN224 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 84 |
| Details | TRANSMEM: Helical; Name=Segment S2 => ECO:0000255 |
| Chain | Residue | Details |
| A | LEU225-SER246 | |
| B | LEU225-SER246 | |
| D | LEU225-SER246 | |
| C | LEU225-SER246 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 84 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:P63142 |
| Chain | Residue | Details |
| A | SER247-LYS255 | |
| A | LEU313-GLU326 | |
| B | SER247-LYS255 | |
| B | LEU313-GLU326 | |
| D | SER247-LYS255 | |
| D | LEU313-GLU326 | |
| C | SER247-LYS255 | |
| C | LEU313-GLU326 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S3 => ECO:0000250|UniProtKB:P63142 |
| Chain | Residue | Details |
| A | GLY256-THR276 | |
| B | GLY256-THR276 | |
| D | GLY256-THR276 | |
| C | GLY256-THR276 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 84 |
| Details | TRANSMEM: Helical; Voltage-sensor; Name=Segment S4 => ECO:0000250|UniProtKB:P63142 |
| Chain | Residue | Details |
| A | VAL291-GLY312 | |
| B | VAL291-GLY312 | |
| D | VAL291-GLY312 | |
| C | VAL291-GLY312 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S5 => ECO:0000250|UniProtKB:P63142 |
| Chain | Residue | Details |
| A | LEU327-PHE347 | |
| B | LEU327-PHE347 | |
| D | LEU327-PHE347 | |
| C | LEU327-PHE347 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 44 |
| Details | INTRAMEM: Helical; Name=Pore helix => ECO:0000250|UniProtKB:P63142 |
| Chain | Residue | Details |
| A | PRO361-THR372 | |
| B | PRO361-THR372 | |
| D | PRO361-THR372 | |
| C | PRO361-THR372 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 28 |
| Details | INTRAMEM: INTRAMEM => ECO:0000250|UniProtKB:P63142 |
| Chain | Residue | Details |
| A | THR373-TYR380 | |
| B | THR373-TYR380 | |
| D | THR373-TYR380 | |
| C | THR373-TYR380 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 112 |
| Details | TRANSMEM: Helical; Name=Segment S6 => ECO:0000250|UniProtKB:P63142 |
| Chain | Residue | Details |
| A | ILE388-TYR416 | |
| B | ILE388-TYR416 | |
| D | ILE388-TYR416 | |
| C | ILE388-TYR416 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:16917065, ECO:0000269|PubMed:18690023 |
| Chain | Residue | Details |
| A | SER11 | |
| A | SER537 | |
| B | SER11 | |
| B | SER537 | |
| D | SER11 | |
| D | SER537 | |
| C | SER11 | |
| C | SER537 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine; by Src => ECO:0000269|PubMed:12615930, ECO:0000269|PubMed:19622611 |
| Chain | Residue | Details |
| A | TYR124 | |
| B | TYR124 | |
| D | TYR124 | |
| C | TYR124 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q03717 |
| Chain | Residue | Details |
| A | SER440 | |
| B | SER440 | |
| D | SER440 | |
| C | SER440 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:16917065, ECO:0000269|PubMed:17192433, ECO:0000269|PubMed:18690023 |
| Chain | Residue | Details |
| A | SER453 | |
| B | SER453 | |
| D | SER453 | |
| C | SER453 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:16917065, ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| A | SER480 | |
| B | SER480 | |
| D | SER480 | |
| C | SER480 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:16917065 |
| Chain | Residue | Details |
| A | SER492 | |
| C | SER492 | |
| C | SER499 | |
| C | SER586 | |
| A | SER499 | |
| A | SER586 | |
| B | SER492 | |
| B | SER499 | |
| B | SER586 | |
| D | SER492 | |
| D | SER499 | |
| D | SER586 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| A | SER515 | |
| B | SER515 | |
| D | SER515 | |
| C | SER515 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by CDK5; in vitro => ECO:0000269|PubMed:16917065, ECO:0000269|PubMed:21712386, ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| A | SER516 | |
| B | SER516 | |
| D | SER516 | |
| C | SER516 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:16917065, ECO:0000269|PubMed:17192433 |
| Chain | Residue | Details |
| A | SER563 | |
| B | SER563 | |
| D | SER563 | |
| C | SER563 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q14721 |
| Chain | Residue | Details |
| A | SER589 | |
| B | SER589 | |
| D | SER589 | |
| C | SER589 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:21518833 |
| Chain | Residue | Details |
| A | LYS470 | |
| B | LYS470 | |
| D | LYS470 | |
| C | LYS470 |
