Q13454: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3 (TUSC3)

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3 (TUSC3) is a 348-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13454.

Gene
TUSC3
Organism
Homo sapiens
Length
348 residues
Mean pLDDT
84.8
Model
AF-Q13454-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.8 (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 accurate56%
70 to 90Confident: backbone generally right31%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions7%

What pLDDT means and how to read it

Function

Acts as accessory component of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Involved in N-glycosylation of STT3B-dependent substrates. Specifically required for the glycosylation of a subset of acceptor sites that are near cysteine residues; in this function seems to act redundantly with MAGT1. In its oxidized form proposed to form transient mixed disulfides with a glycoprotein substrate to facilitate access of STT3B to the unmodified acceptor site. Also has oxidoreductase-independent…

Subunit structure

Accessory component of the STT3B-containing form of the oligosaccharyltransferase (OST) complex. OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes.…

Subcellular location

Endoplasmic reticulum membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4M91X-ray1.1 ÅA=44-194
4M90X-ray1.6 ÅA=44-194
4M92X-ray1.6 ÅA=44-194
4M8GX-ray2.0 ÅA/B=44-194

More AlphaFold highlights

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