Q6Z156: Protein PHOSPHATE STARVATION RESPONSE 2 (PHR2)

Protein PHOSPHATE STARVATION RESPONSE 2 (PHR2) is a 426-residue protein from Oryza sativa subsp. japonica. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q6Z156.

Gene
PHR2
Organism
Oryza sativa subsp. japonica
Length
426 residues
Mean pLDDT
57.1
Model
AF-Q6Z156-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 57.1 (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 accurate20%
70 to 90Confident: backbone generally right3%
50 to 70Low: treat with caution19%
Below 50Very low: often disordered regions58%

What pLDDT means and how to read it

Function

Transcription factor involved in phosphate starvation signaling (PubMed:18263782, PubMed:26082401). Binds to P1BS, an imperfect palindromic sequence 5'-GNATATNC-3', to promote the expression of inorganic phosphate (Pi) starvation-responsive genes (PubMed:25657119, PubMed:26082401). Functionally redundant with PHR1 and PHR3 in regulating Pi starvation response and Pi homeostasis (PubMed:26082401). Involved in both systematic and local Pi-signaling pathways (PubMed:19704822). Regulates several Pi transporters (PubMed:18263782). Regulates the expression of PT2 (PubMed:20149131). Directly up-regulates SPX1 and SPX2 expression, but PHR2 binding to DNA is repressed redundantly by SPX1 and SPX2…

Subunit structure

Interacts (via C-terminus) with SPX4 (via N-terminus) in the presence of inositol polyphosphate (PubMed:24692424, PubMed:27080106). Interacts (via C-terminus) with SPX1 and SPX2 (via SPX domain) (PubMed:25271318, PubMed:35640569). Interacts with RLI1 isoform RLI1b in the nucleus (PubMed:35640569)

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7E40X-ray2.6 ÅA/C=248-380
7D3YX-ray3.11 ÅC/D/E=225-362

More AlphaFold highlights

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