P61011: Signal recognition particle subunit SRP54 (SRP54)

Signal recognition particle subunit SRP54 (SRP54) is a 504-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61011.

Gene
SRP54
Organism
Homo sapiens
Length
504 residues
Mean pLDDT
79.3
Model
AF-P61011-F1 v6
Model created
1 Aug 2025
PDB structures
9

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 79.3 (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 accurate28%
70 to 90Confident: backbone generally right46%
50 to 70Low: treat with caution20%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:34020957). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane (PubMed:34020957). Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes (PubMed:34020957). Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA (PubMed:28972538, PubMed:34020957). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with…

Subunit structure

Component of a signal recognition particle (SRP) complex that consists of a 7SL RNA molecule of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9 (PubMed:12244299). Interacts with RNPS1 (PubMed:14729963). Interacts with the SRP receptor subunit SRPRA (PubMed:34020957)

Subcellular location

Nucleus speckle, Cytoplasm, Endoplasmic reticulum

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1QB2X-ray2.1 ÅA/B=326-434
6Y2ZX-ray2.15 ÅA/B=1-296
6Y32X-ray2.6 ÅA/C/E/G=1-296
6Y30X-ray2.65 ÅA/B=1-296
7QWQEM2.83 Åx=1-504
1MFQX-ray3.1 ÅC=323-441
5L3QX-ray3.2 ÅA/C=1-436
7NFXEM3.2 Åx=1-504
6Y31X-ray4.0 ÅA/B/C/D=1-296

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.