P48432: Transcription factor SOX-2 (Sox2)

Transcription factor SOX-2 (Sox2) is a 319-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P48432.

Gene
Sox2
Organism
Mus musculus
Length
319 residues
Mean pLDDT
59.5
Model
AF-P48432-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 59.5 (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 accurate23%
70 to 90Confident: backbone generally right3%
50 to 70Low: treat with caution22%
Below 50Very low: often disordered regions52%

What pLDDT means and how to read it

Function

Transcription factor that forms a trimeric complex with POU5F1 (OCT3/4) on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 (PubMed:15863505, PubMed:17097055, PubMed:19740739, PubMed:32703285). Binds to the proximal enhancer region of NANOG (PubMed:15863505). Critical for early embryogenesis and for embryonic stem cell pluripotency (By similarity). Downstream SRRT target that mediates the promotion of neural stem cell self-renewal (PubMed:22198669). Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity). May function as a switch…

Subunit structure

Interacts with ZSCAN10 (PubMed:19740739). Interacts with SOX3 and FGFR1 (PubMed:17728342). Interacts with GLIS1 (By similarity). Interacts with POU5F1; binds synergistically with POU5F1 to DNA (PubMed:15863505). Interacts with DDX56 (PubMed:32703285). Interacts with L3MBTL3 and DCAF5 (PubMed:30442713). The interaction with L3MBTL3 and DCAF5 requires methylation at Lys-44 and is necessary to…

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8BX1X-ray2.5 ÅE=41-120
1GT0X-ray2.6 ÅD=41-120
8BX2X-ray3.14 ÅE=41-120
6HT5X-ray3.45 ÅD=41-120

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