P48349: 14-3-3-like protein G-BOX factor 14 lambda (GRF6)

14-3-3-like protein G-BOX factor 14 lambda (GRF6) is a 248-residue protein from Arabidopsis thaliana. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P48349.

Gene
GRF6
Organism
Arabidopsis thaliana
Length
248 residues
Mean pLDDT
96.3
Model
AF-P48349-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 96.3 (very high 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 accurate92%
70 to 90Confident: backbone generally right7%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes (By similarity). Specific negative regulator of slow-vacuolar (SV) ion channel. Mediates F-actin dynamics possibly through inhibiting ADF1 phosphorylation (PubMed:26345162). Negative regulator of freezing tolerance that modulates cold-responsive C-repeat-binding factors (CBF) DREB1A and DREB1B proteins stability by facilitating their ubiquitin-mediated degradation when activated by CRPK1-mediated phosphorylation in freezing conditions; this processus is counteracted by B1L (PubMed:28344081, PubMed:31297122)

Subunit structure

Interacts with SERK1 in the cell membrane. Component of the SERK1 signaling complex, composed of KAPP, CDC48A, GRF6 or GRF7, SERK1, SERK2, SERK3/BAK1 and BRI1 (PubMed:15592873). Interacts with TPK1 (PubMed:17764516). Interacts with ADF1 (PubMed:26345162). Binds to CRPK1 at the plasma membrane. Interacts with DREB1A and DREB1B in the nucleus when activated by CRPK1-mediated phosphorylation upon…

Subcellular location

Nucleus, Cell membrane, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8QT5X-ray2.69 ÅA/B/C/D/E/F/G=1-248

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