P38377: Protein transport protein Sec61 subunit alpha isoform 1 (SEC61A1)

Protein transport protein Sec61 subunit alpha isoform 1 (SEC61A1) is a 476-residue protein from Canis lupus familiaris. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P38377.

Gene
SEC61A1
Organism
Canis lupus familiaris
Length
476 residues
Mean pLDDT
73.4
Model
AF-P38377-F1 v6
Model created
1 Aug 2025
PDB structures
19

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.4 (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 accurate0%
70 to 90Confident: backbone generally right66%
50 to 70Low: treat with caution31%
Below 50Very low: often disordered regions4%

What pLDDT means and how to read it

Function

Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER) (PubMed:10799540, PubMed:1423609). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (By similarity). May cooperate with auxiliary protein SEC62, SEC63 and HSPA5/BiP to enable post-translational transport of small presecretory proteins (By similarity). The SEC61 channel is also involved in ER membrane insertion of transmembrane proteins: it mediates membrane insertion of the first few transmembrane segments of proteins, while…

Subunit structure

The SEC61 channel-forming translocon complex consists of channel-forming core components SEC61A1, SEC61B and SEC61G and different auxiliary components such as SEC62 and SEC63 (PubMed:10799540, PubMed:1423609, PubMed:36261528). The SEC61 channel associates with the multi-pass translocon (MPT) complex (PubMed:36261528)

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
6Z3TEM2.69 ÅA=1-476
8RJBEM2.69 Å1=1-476
8RJDEM2.79 Å1=1-476
8RJCEM2.9 Å1=1-476
7TM3EM3.25 Å1=1-476
8OJ0EM3.3 Å1=1-476
8OJ8EM3.3 Å1=1-476
8BTKEM3.5 ÅSX=1-476
3JC2EM3.6 Å1=1-476
7TUTEM3.88 Å1=1-476
6R7QEM3.9 ÅXX=5-465
6FTIEM4.2 Åx=5-465
6FTJEM4.7 Åx=5-465
2WWBEM6.48 ÅA=1-476
4CG7EM6.9 ÅA=1-476
4CG5EM7.4 ÅA=1-476
4CG6EM7.8 ÅA=1-476
5A6UEM9.0 ÅA=26-476
6FTGEM9.1 Åx=5-465

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