P61619: Protein transport protein Sec61 subunit alpha isoform 1 (SEC61A1)

Protein transport protein Sec61 subunit alpha isoform 1 (SEC61A1) is a 476-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61619.

Gene
SEC61A1
Organism
Homo sapiens
Length
476 residues
Mean pLDDT
72.9
Model
AF-P61619-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 72.9 (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 right64%
50 to 70Low: treat with caution33%
Below 50Very low: often disordered regions3%

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:12475939, PubMed:22375059, PubMed:28782633, PubMed:29719251, PubMed:32814900). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (PubMed:22375059, PubMed:28782633, PubMed:29719251). May cooperate with auxiliary protein SEC62, SEC63 and HSPA5/BiP to enable post-translational transport of small presecretory proteins (PubMed:22375059, PubMed:29719251). The SEC61 channel is also involved in ER membrane insertion of…

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:36697828). The SEC61 channel associates with the multi-pass translocon (MPT) complex (PubMed:32820719, PubMed:36261522)

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
8DNZEM2.57 ÅA=1-476
8DNYEM2.85 ÅA=1-476
8DO0EM2.86 ÅA=1-476
8DO2EM2.95 ÅA=1-476
8DNXEM2.98 ÅA=1-476
8DO1EM3.01 ÅA=1-476
8DNVEM3.03 ÅA=1-476
9D6LEM3.1 ÅA=1-476
9N9JEM3.2 ÅD=1-476
8DO3EM3.22 ÅA=1-476
8DNWEM3.4 ÅA=1-476
6W6LEM3.84 Å1=1-476
9YGYEM4.1 ÅD=1-476
8B6LEM7.6 ÅA=1-476

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