Q9LDI3: CBL-interacting serine/threonine-protein kinase 24 (CIPK24)

CBL-interacting serine/threonine-protein kinase 24 (CIPK24) is a 446-residue protein from Arabidopsis thaliana. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9LDI3.

Gene
CIPK24
Organism
Arabidopsis thaliana
Length
446 residues
Mean pLDDT
79.8
Model
AF-Q9LDI3-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.8 (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 accurate38%
70 to 90Confident: backbone generally right38%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions12%

What pLDDT means and how to read it

Function

Involved in the regulatory pathway for the control of intracellular Na(+) and K(+) homeostasis and salt tolerance. Activates the vacuolar H(+)/Ca(2+) antiporter CAX1 and operates in synergy with CBL4/SOS3 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Phosphorylates CBL1, CBL4 and CBL10

Subunit structure

Interacts with CBL1, CBL2, CBL4/SOS3, CBL5, CBL9, CBL10 and with the protein phosphatase 2C ABI2

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2EHBX-ray2.1 ÅD=304-446
4D28X-ray3.3 ÅA/B/C/D=1-446

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