Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

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	80
Details	Transmembrane: {"description":"Helical; Signal-anchor for type II membrane protein","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15476821","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	140
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	140
Details	Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	52
Details	Region: {"description":"Interaction with KCND2","evidences":[{"source":"UniProtKB","id":"Q8R426","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17057713","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17187064","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	84
Details	Transmembrane: {"description":"Helical; Name=Segment S1","evidences":[{"source":"PubMed","id":"34552243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7F0J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	88
Details	Transmembrane: {"description":"Helical; Name=Segment S2","evidences":[{"source":"PubMed","id":"34552243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7F0J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	76
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"34552243","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	96
Details	Transmembrane: {"description":"Helical; Name=Segment S3","evidences":[{"source":"PubMed","id":"34552243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7F0J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	72
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"34552243","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	76
Details	Transmembrane: {"description":"Helical; Voltage-sensor; Name=Segment S4","evidences":[{"source":"PubMed","id":"34552243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7F0J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	92
Details	Transmembrane: {"description":"Helical; Name=Segment S5","evidences":[{"source":"PubMed","id":"34552243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7F0J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	44
Details	Intramembrane: {"description":"Helical; Name=Pore helix","evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	28
Details	Intramembrane: {"evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	88
Details	Transmembrane: {"description":"Helical; Name=Segment S6","evidences":[{"source":"PubMed","id":"34552243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7F0J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	72
Details	Region: {"description":"Interaction with KCNIP1, KCNIP2, and other family members","evidences":[{"source":"UniProtKB","id":"Q63881","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	76
Details	Region: {"description":"Interaction with KCNIP1","evidences":[{"source":"UniProtKB","id":"Q63881","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	52
Details	Region: {"description":"S4-S5 linker","evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	60
Details	Region: {"description":"Required for dendritic targeting","evidences":[{"source":"UniProtKB","id":"Q63881","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	20
Details	Motif: {"description":"Selectivity filter","evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	12
Details	Binding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"34552243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7F0J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	4
Details	Binding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"34552243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7F0J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35597238","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7UK5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UKD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UKE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UKF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35597238","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7UKC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UKG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35597238","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7UK5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UKC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UKD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UKE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UKF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UKG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q63881","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q63881","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)