Q9H2S1: Small conductance calcium-activated potassium channel protein 2 (KCNN2)

Small conductance calcium-activated potassium channel protein 2 (KCNN2) is a 579-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9H2S1.

Gene
KCNN2
Organism
Homo sapiens
Length
579 residues
Mean pLDDT
76.5
Model
AF-Q9H2S1-F1 v6
Model created
1 Aug 2025
PDB structures
15

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Model confidence (pLDDT)

The mean pLDDT of this model is 76.5 (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 accurate43%
70 to 90Confident: backbone generally right30%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions23%

What pLDDT means and how to read it

Function

Small conductance calcium-activated potassium channel that mediates the voltage-independent transmembrane transfer of potassium across the cell membrane through a constitutive interaction with calmodulin which binds the intracellular calcium allowing its opening (PubMed:10991935, PubMed:33242881, PubMed:9287325). The current is characterized by a voltage-independent activation, an intracellular calcium concentration increase-dependent activation and a single-channel conductance of about 3 picosiemens (PubMed:10991935). Also presents an inwardly rectifying current, thus reducing its already small outward conductance of potassium ions, which is particularly the case when the membrane…

Subunit structure

Homodimer (PubMed:20689065). Heteromultimer with KCNN1 and KCNN3 (PubMed:20689065, PubMed:9287325). The complex is composed of 4 channel subunits each of which binds to a calmodulin subunit which regulates the channel activity through calcium-binding (By similarity). Interacts (via N-terminal domain) with MPP2 (By similarity)

Subcellular location

Membrane, Cytoplasm, myofibril, sarcomere, Z line

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5V03X-ray1.58 ÅB=395-486
5V02X-ray1.78 ÅB=395-486
5WBXX-ray1.9 ÅB=395-486
5WC5X-ray2.3 ÅB=395-486
6ALEX-ray2.5 ÅB=394-486
9ZRQEM2.77 ÅA/B/C/D=117-477
9VUCEM2.96 ÅA/B/C/D=1-579
9O48EM3.1 ÅA/B/C/D=125-412
9O5OEM3.1 ÅA/B/C/D=125-412
9O52EM3.18 ÅA/B/C/D=125-412
9VUAEM3.23 ÅA/B/C/D=1-579
9O53EM3.3 ÅA/B/C/D=125-412
9VU9EM3.34 ÅA/B/C/D=1-579
9VUBEM3.35 ÅA/B/C/D=1-579
9O51EM3.4 ÅA/B/C/D=125-412

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