O24646: Transcription factor HY5 (HY5)

Transcription factor HY5 (HY5) is a 168-residue protein from Arabidopsis thaliana. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O24646.

Gene
HY5
Organism
Arabidopsis thaliana
Length
168 residues
Mean pLDDT
69.0
Model
AF-O24646-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 69.0 (low 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 right4%
50 to 70Low: treat with caution27%
Below 50Very low: often disordered regions31%

What pLDDT means and how to read it

Function

Transcription factor that promotes photomorphogenesis in light. Acts downstream of the light receptor network and directly affects transcription of light-induced genes. Specifically involved in the blue light specific pathway, suggesting that it participates in transmission of cryptochromes (CRY1 and CRY2) signals to downstream responses. In darkness, its degradation prevents the activation of light-induced genes (Probable). Involved in responses to cold conditions probably by modulating the expression of several genes and triggering anthocyanin biosynthesis (PubMed:28412546). Acts coordinately with SPL7 to regulate the microRNA miR408 and its target genes in response to changes in light…

Subunit structure

Homodimer; homodimerizes via the leucine-zipper domains (PubMed:17261584). Heterodimer; heterodimerizes with HYH via the leucine-zipper domains (PubMed:12023303). Interacts with COP1 WD40 domain (PubMed:11226162). Interacts with BBX21 (PubMed:21632973), BBX24/STO (PubMed:23733077) and BBX25/STH (PubMed:23624715). Interacts with SPL7 (PubMed:25516599). Binds to SHW1 in the nucleus…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6QTOX-ray1.27 ÅB=39-49
6QTRX-ray1.37 ÅB=39-49
5KWNX-ray1.42 ÅU=34-52
2OQQX-ray2.0 ÅA/B=111-150

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