P61010: Signal recognition particle subunit SRP54 (SRP54)

Signal recognition particle subunit SRP54 (SRP54) is a 504-residue protein from Canis lupus familiaris. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61010.

Gene
SRP54
Organism
Canis lupus familiaris
Length
504 residues
Mean pLDDT
78.6
Model
AF-P61010-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 78.6 (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 accurate27%
70 to 90Confident: backbone generally right46%
50 to 70Low: treat with caution21%
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:6413076, PubMed:6938958). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane (By similarity). Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes (By similarity). Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA (By similarity). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR…

Subunit structure

Component of a signal recognition particle complex that consists of a 7SL RNA molecule of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9 (PubMed:6413076, PubMed:6938958). Interacts with RNPS1 (By similarity). Interacts with the SRP receptor subunit SRPRA (By similarity)

Subcellular location

Nucleus speckle, Cytoplasm, Endoplasmic reticulum

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7OBREM2.8 Åx=1-504
6FRKEM3.7 Åx=1-504
6R6GEM3.7 ÅAB=4-434
7OBQEM3.9 Åx=1-504
2GO5EM7.4 ÅW=326-434
2J37EM8.0 ÅW=1-504
4UE5EM9.0 ÅD=1-433

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