7E8H
CryoEM structure of human Kv4.2-DPP6S-KChIP1 complex
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 |
E | 0005509 | molecular_function | calcium ion binding |
F | 0005509 | molecular_function | calcium ion binding |
G | 0005509 | molecular_function | calcium ion binding |
H | 0005509 | molecular_function | calcium ion binding |
I | 0006508 | biological_process | proteolysis |
I | 0008236 | molecular_function | serine-type peptidase activity |
J | 0006508 | biological_process | proteolysis |
J | 0008236 | molecular_function | serine-type peptidase activity |
K | 0006508 | biological_process | proteolysis |
K | 0008236 | molecular_function | serine-type peptidase activity |
L | 0006508 | biological_process | proteolysis |
L | 0008236 | molecular_function | serine-type peptidase activity |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DINKDGYINkeEM |
Chain | Residue | Details |
E | ASP135-MET147 | |
E | ASP183-PHE195 | |
F | ASP135-MET147 | |
F | ASP183-PHE195 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:17057713, ECO:0000269|PubMed:17187064 |
Chain | Residue | Details |
E | ASP135 | |
G | ASP135 | |
G | ASN137 | |
G | ASP139 | |
G | TYR141 | |
G | GLU146 | |
G | ASP183 | |
G | ASN185 | |
G | ASP187 | |
G | GLU194 | |
E | ASN137 | |
E | ASP139 | |
E | TYR141 | |
E | GLU146 | |
E | ASP183 | |
E | ASN185 | |
E | ASP187 | |
E | GLU194 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15476821 |
Chain | Residue | Details |
J | ASN111 | |
L | ASN473 | |
L | ASN504 | |
L | ASN751 | |
C | GLU205-ALA228 | |
C | THR280-SER286 | |
C | TYR344-ILE357 | |
C | PRO378-LYS384 | |
J | ASN257 | |
J | ASN342 | |
J | ASN473 | |
J | ASN504 | |
J | ASN751 | |
L | ASN111 | |
L | ASN257 | |
L | ASN342 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
J | ASN409 | |
L | ASN409 | |
D | PHE229-ALA250 | |
C | PHE229-ALA250 |
site_id | SWS_FT_FI4 |
Number of Residues | 96 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:P63142 |
Chain | Residue | Details |
B | ALA251-VAL261 | |
B | SER307-ALA321 | |
A | ALA251-VAL261 | |
A | SER307-ALA321 | |
D | ALA251-VAL261 | |
D | SER307-ALA321 | |
C | ALA251-VAL261 | |
C | SER307-ALA321 |
site_id | SWS_FT_FI5 |
Number of Residues | 68 |
Details | TRANSMEM: Helical; Name=Segment S3 => ECO:0000250|UniProtKB:P63142 |
Chain | Residue | Details |
B | MET262-MET279 | |
A | MET262-MET279 | |
D | MET262-MET279 | |
C | MET262-MET279 |
site_id | SWS_FT_FI6 |
Number of Residues | 76 |
Details | TRANSMEM: Helical; Voltage-sensor; Name=Segment S4 => ECO:0000250|UniProtKB:P63142 |
Chain | Residue | Details |
B | GLY287-HIS306 | |
A | GLY287-HIS306 | |
D | GLY287-HIS306 | |
C | GLY287-HIS306 |
site_id | SWS_FT_FI7 |
Number of Residues | 84 |
Details | TRANSMEM: Helical; Name=Segment S5 => ECO:0000250|UniProtKB:P63142 |
Chain | Residue | Details |
B | SER322-PHE343 | |
A | SER322-PHE343 | |
D | SER322-PHE343 | |
C | SER322-PHE343 |
site_id | SWS_FT_FI8 |
Number of Residues | 44 |
Details | INTRAMEM: Helical; Name=Pore helix => ECO:0000250|UniProtKB:P63142 |
Chain | Residue | Details |
B | PRO358-THR369 | |
A | PRO358-THR369 | |
D | PRO358-THR369 | |
C | PRO358-THR369 |
site_id | SWS_FT_FI9 |
Number of Residues | 28 |
Details | INTRAMEM: INTRAMEM => ECO:0000250|UniProtKB:P63142 |
Chain | Residue | Details |
B | THR370-VAL377 | |
A | THR370-VAL377 | |
D | THR370-VAL377 | |
C | THR370-VAL377 |
site_id | SWS_FT_FI10 |
Number of Residues | 112 |
Details | TRANSMEM: Helical; Name=Segment S6 => ECO:0000250|UniProtKB:P63142 |
Chain | Residue | Details |
B | ILE385-TYR413 | |
A | ILE385-TYR413 | |
D | ILE385-TYR413 | |
C | ILE385-TYR413 |
site_id | SWS_FT_FI11 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q63881 |
Chain | Residue | Details |
B | HIS105 | |
C | HIS105 | |
C | CYS132 | |
C | CYS133 | |
B | CYS132 | |
B | CYS133 | |
A | HIS105 | |
A | CYS132 | |
A | CYS133 | |
D | HIS105 | |
D | CYS132 | |
D | CYS133 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q63881 |
Chain | Residue | Details |
B | THR38 | |
A | THR38 | |
D | THR38 | |
C | THR38 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q63881 |
Chain | Residue | Details |
B | SER438 | |
A | SER438 | |
D | SER438 | |
C | SER438 |