O35718: Suppressor of cytokine signaling 3 (Socs3)

Suppressor of cytokine signaling 3 (Socs3) is a 225-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O35718.

Gene
Socs3
Organism
Mus musculus
Length
225 residues
Mean pLDDT
69.0
Model
AF-O35718-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 accurate8%
70 to 90Confident: backbone generally right53%
50 to 70Low: treat with caution17%
Below 50Very low: often disordered regions22%

What pLDDT means and how to read it

Function

SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway (By similarity). Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including IL6ST/gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors (PubMed:10821852, PubMed:12754505, PubMed:9889194). Binding to JAK2 inhibits its kinase activity and regulates IL6 signaling (PubMed:12754505, PubMed:9889194). Suppresses fetal liver erythropoiesis (PubMed:10490101). Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells…

Subunit structure

Interacts with multiple activated proteins of the tyrosine kinase signaling pathway including IGF1 receptor, insulin receptor and JAK2. Binding to JAK2 is mediated through the KIR and SH2 domains to a phosphorylated tyrosine residue within the JAK2 JH1 domain (By similarity). Binds specific activated tyrosine residues of the leptin, EPO, IL12, GSCF and gp130 receptors (PubMed:10882725).…

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2HMHX-ray2.0 ÅA=15-185
4GL9X-ray3.9 ÅE/F/G/H=38-128
2BBUNMRA=22-185
2JZ3NMRA=186-225

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