P43307: Translocon-associated protein subunit alpha (SSR1)

Translocon-associated protein subunit alpha (SSR1) is a 286-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P43307.

Gene
SSR1
Organism
Homo sapiens
Length
286 residues
Mean pLDDT
76.1
Model
AF-P43307-F1 v6
Model created
1 Aug 2025
PDB structures
3

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 76.1 (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 accurate47%
70 to 90Confident: backbone generally right16%
50 to 70Low: treat with caution19%
Below 50Very low: often disordered regions19%

What pLDDT means and how to read it

Function

TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins

Subunit structure

Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-gamma (PubMed:36697828). Interacts with palmitoylated calnexin (CALX), the interaction is required for efficient folding of glycosylated proteins (PubMed:22314232)

Subcellular location

Endoplasmic reticulum membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9N9JEM3.2 Å5=1-286
9YGYEM4.1 Å5=1-286
8B6LEM7.6 ÅE=1-286

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.