O76094: Signal recognition particle subunit SRP72 (SRP72)

Signal recognition particle subunit SRP72 (SRP72) is a 671-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O76094.

Gene
SRP72
Organism
Homo sapiens
Length
671 residues
Mean pLDDT
81.8
Model
AF-O76094-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.8 (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 accurate65%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions17%

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). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER (PubMed:34020957). The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (PubMed:34020957). Binds the signal recognition particle RNA (7SL RNA) in presence of SRP68…

Subunit structure

Heterodimer with SRP68 (PubMed:16672232, PubMed:27899666, PubMed:28369529). SRP68-SRP72 heterodimer formation is stabilized by the presence of 7SL RNA (By similarity). 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 (By similarity). Within the SRP complex,…

Subcellular location

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
5M72X-ray1.6 ÅA=10-166
5WRVX-ray1.7 ÅB=1-163
8QVXEM2.7 ÅB=1-671
5WRWX-ray2.91 ÅA/B/C/D/E/F=1-163
8QVWEM3.0 ÅB=1-671
7NFXEM3.2 Åz=1-671
5M73X-ray3.4 ÅD/H=512-668

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