P63252: Inward rectifier potassium channel 2 (KCNJ2)

Inward rectifier potassium channel 2 (KCNJ2) is a 427-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P63252.

Gene
KCNJ2
Organism
Homo sapiens
Length
427 residues
Mean pLDDT
81.6
Model
AF-P63252-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.6 (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 accurate66%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions19%

What pLDDT means and how to read it

Function

Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it (PubMed:36149965, PubMed:7590287, PubMed:9490857). Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages (PubMed:7590287, PubMed:7696590). The inward rectification is mainly due to the blockage of outward current by internal magnesium (PubMed:9490857). Can be blocked by extracellular barium or cesium (PubMed:7590287, PubMed:7696590). Probably participates in establishing action potential waveform and excitability of…

Subunit structure

Homotetramer (PubMed:36149965, PubMed:16571646). Homomultimeric and heteromultimeric association with KCNJ4/Kir2.3 (PubMed:12032359). Can form heteromeric channels with Kir2.6/KCNJ18 (PubMed:21209095). Associates, via its PDZ-recognition domain, with a complex containing LIN7A, LIN7B, LIN7C, DLG1, CASK and APBA1 (By similarity)

Subcellular location

Cell membrane, Cell membrane, sarcolemma, T-tubule

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6SPZX-ray2.08 ÅP/Q=422-427
7ZDZEM4.3 ÅA/B/C/D=1-427
8QQLEM6.0 ÅA/B/C/D=46-362

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