O88703: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (Hcn2)

Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (Hcn2) is a 863-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O88703.

Gene
Hcn2
Organism
Mus musculus
Length
863 residues
Mean pLDDT
71.0
Model
AF-O88703-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 71.0 (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 accurate37%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions34%

What pLDDT means and how to read it

Function

Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih) (PubMed:10962006, PubMed:11096117, PubMed:11459060, PubMed:11741901, PubMed:12034718, PubMed:12193608, PubMed:12968185, PubMed:17562314, PubMed:21347269, PubMed:21903816, PubMed:23103389). Can also transport ammonium in the distal nephron (By similarity). Involved in the initiation of neuropathic pain in sensory neurons (PubMed:21903816)

Subunit structure

Homotetramer (Probable) (PubMed:12968185, PubMed:18367452, PubMed:19525958). The channel is composed of a homo- or heterotetrameric complex of pore-forming subunits (PubMed:12034718, PubMed:12928435, PubMed:12968185, PubMed:18367452). Heterotetramer with HCN1 (PubMed:12034718, PubMed:12928435). Forms an obligate 4:4 complex with accessory subunit PEX5L; regulates HCN2 cell-surface expression and…

Subcellular location

Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3BPZX-ray1.65 ÅA/B/C/D=443-640
5KHHX-ray1.77 ÅA=443-643
1Q3EX-ray1.9 ÅA/B=443-645
3ETQX-ray1.9 ÅA/B=443-640
1Q43X-ray2.0 ÅA/B=443-645
5KHJX-ray2.01 ÅA/B=443-643
5JONX-ray2.04 ÅA/B=494-640
5KHKX-ray2.07 ÅA=443-643
5KHIX-ray2.1 ÅA=443-643
5KHGX-ray2.24 ÅA=443-643
2Q0AX-ray2.25 ÅA/B=443-640
1Q5OX-ray2.3 ÅA=443-645
3FFQX-ray2.4 ÅA/B=443-640
4EQFX-ray3.0 ÅB=857-863

More AlphaFold highlights

About this viewer

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