P15382: Potassium voltage-gated channel subfamily E member 1 (KCNE1)

Potassium voltage-gated channel subfamily E member 1 (KCNE1) is a 129-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P15382.

Gene
KCNE1
Organism
Homo sapiens
Length
129 residues
Mean pLDDT
70.6
Model
AF-P15382-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 70.6 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate14%
70 to 90Confident: backbone generally right36%
50 to 70Low: treat with caution41%
Below 50Very low: often disordered regions9%

What pLDDT means and how to read it

Function

Ancillary protein that functions as a regulatory subunit of the voltage-gated potassium (Kv) channel complex composed of pore-forming and potassium-conducting alpha subunits and of regulatory beta subunits. KCNE1 beta subunit modulates the gating kinetics and enhances stability of the channel complex (PubMed:19219384, PubMed:20533308, PubMed:9230439). Alters the gating of the delayed rectifier Kv channel containing KCNB1 alpha subunit (PubMed:19219384). Associates with KCNQ1/KVLQT1 alpha subunit to form the slowly activating delayed rectifier cardiac potassium (IKs) channel responsible for ventricular muscle action potential repolarization (PubMed:20533308). The outward current reaches its…

Subunit structure

Interacts with KCNB1. Interacts with KCNC2 (By similarity). Associates with KCNH2/HERG (PubMed:9230439). Interacts with KNCQ1; targets the complex KNCQ1-KCNE1 to the membrane raft (PubMed:20533308). The complex KNCQ1-KNCE1 interacts with the scolopendra toxin SSD609 (PubMed:26307551)

Subcellular location

Cell membrane, Apical cell membrane, Membrane raft

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
9VECEM2.7 ÅC/F/I/L=1-129
9U7FEM2.9 ÅC/F/I/L=1-129
9UC8EM3.36 ÅC/F/I/L=39-68
9VEIEM3.9 ÅC/F/I/L=1-129
2K21NMRA=1-129

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