P48431: Transcription factor SOX-2 (SOX2)

Transcription factor SOX-2 (SOX2) is a 317-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P48431.

Gene
SOX2
Organism
Homo sapiens
Length
317 residues
Mean pLDDT
59.8
Model
AF-P48431-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 59.8 (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 right4%
50 to 70Low: treat with caution24%
Below 50Very low: often disordered regions48%

What pLDDT means and how to read it

Function

Transcription factor that forms a trimeric complex with OCT4 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 (By similarity). Binds to the proximal enhancer region of NANOG (By similarity). Critical for early embryogenesis and for embryonic stem cell pluripotency (PubMed:18035408). Downstream SRRT target that mediates the promotion of neural stem cell self-renewal (By similarity). Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity). May function as a switch in neuronal development (By similarity)

Subunit structure

Interacts with ZSCAN10 (By similarity). Interacts with SOX3 and FGFR1 (By similarity). Interacts with GLIS1 (PubMed:21654807). Interacts with POU5F1; binds synergistically with POU5F1 to DNA (By similarity). Interacts with DDX56 (By similarity). Interacts with L3MBTL3 and DCAF5; the interaction requires methylation at Lys-42 and is necessary to target SOX2 for ubiquitination by the CRL4-DCAF5 E3…

Subcellular location

Nucleus speckle, Cytoplasm, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6WX8X-ray2.3 ÅB/D=39-127
6WX7X-ray2.7 ÅB=39-127
6WX9X-ray2.8 ÅB=39-127
6T90EM3.05 ÅL=37-118
6YOVEM3.42 ÅL=37-118
9RL4EM3.5 ÅW=37-118
9RN2EM4.1 ÅW=37-118
9RMCEM4.2 ÅW=37-118
6T7BEM5.1 ÅK=36-121
9RN1EM5.9 ÅW=37-118
1O4XNMRB=39-121
2LE4NMRA=39-118
9QPFNMRA=33-127

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