P13664: Major surface antigen p30 (SAG1)

Major surface antigen p30 (SAG1) is a 336-residue protein from Toxoplasma gondii. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P13664.

Gene
SAG1
Organism
Toxoplasma gondii
Length
336 residues
Mean pLDDT
81.4
Model
AF-P13664-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.4 (confident 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 accurate63%
70 to 90Confident: backbone generally right12%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions19%

What pLDDT means and how to read it

Function

Mediates binding to host cells and is especially important for parasite attachment and fitness in IFN-gamma/IFNG-stimulated host cells (PubMed:15151144, PubMed:40607979). May regulate binding between human S100A6 and vimentin (VIM) for cytoskeleton organization during the early stages of invasion into host cells (PubMed:34950858). Promotes TNF secretion in host cells probably by enhancing binding between human VIM and PRKCQ and activating NF-kappa-B pathway (PubMed:34950858). Promotes viability of host cells to satisfy the survival needs of parasites through the interaction with human RACK1 (PubMed:38157925)

Subunit structure

Monomer (PubMed:12091874). Forms homodimers (PubMed:12091874). Interacts with human lysine-rich coiled-coil protein 1 (KRCC1) (PubMed:29351065, PubMed:31165984). Interacts with human S100A6 (PubMed:34950858). Interacts with human RACK1; the interaction promotes viability of host cells (PubMed:38157925)

Subcellular location

Parasitophorous vacuole

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1KZQX-ray1.7 ÅA/B=48-336
1YNTX-ray3.1 ÅF/G=50-303

More AlphaFold highlights

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