P60468: Protein transport protein Sec61 subunit beta (SEC61B)

Protein transport protein Sec61 subunit beta (SEC61B) is a 96-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P60468.

Gene
SEC61B
Organism
Homo sapiens
Length
96 residues
Mean pLDDT
57.5
Model
AF-P60468-F1 v6
Model created
1 Aug 2025
PDB structures
16

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Model confidence (pLDDT)

The mean pLDDT of this model is 57.5 (low 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 accurate5%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution33%
Below 50Very low: often disordered regions47%

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). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (PubMed:12475939). 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 insertion of subsequent transmembrane regions of multi-pass membrane proteins is mediated by the multi-pass translocon (MPT) complex (PubMed:32820719, PubMed:36261522).…

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). Interacts with TRAM1 (PubMed:19121997)

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
8DNZEM2.57 ÅC=1-96
8DNYEM2.85 ÅC=1-96
8DO0EM2.86 ÅC=1-96
8DO2EM2.95 ÅC=1-96
8DNXEM2.98 ÅC=1-96
8DO1EM3.01 ÅC=1-96
8DNVEM3.03 ÅC=1-96
9D6LEM3.1 ÅC=1-96
9N9JEM3.2 ÅE=1-96
8DO3EM3.22 ÅC=1-96
8OJ0EM3.3 Å3=1-96
8OJ8EM3.3 Å3=1-96
8DNWEM3.4 ÅC=1-96
6W6LEM3.84 Å3=1-96
9YGYEM4.1 ÅE=1-96
8B6LEM7.6 ÅB=1-96

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