Signal recognition particle protein (ffh) is a 453-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0AGD7.
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The mean pLDDT of this model is 81.4 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 36% |
| 70 to 90 | Confident: backbone generally right | 42% |
| 50 to 70 | Low: treat with caution | 20% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components
Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY. SRP is a ribonucleoprotein composed of Ffh and a 4.5S RNA molecule. Metal ions are essential for the formation and stability of the SRP complex. Interacts with the ribosomes, via ribosomal protein L23. Interacts with FtsY
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1HQ1 | X-ray | 1.52 Å | A=328-432 |
| 1DUL | X-ray | 1.8 Å | A=328-432 |
| 3LQX | X-ray | 1.93 Å | A=329-428 |
| 2PXB | X-ray | 2.0 Å | A=329-430 |
| 2PXD | X-ray | 2.0 Å | A=329-430 |
| 2PXE | X-ray | 2.0 Å | A=329-430 |
| 2PXF | X-ray | 2.0 Å | A=329-430 |
| 2PXK | X-ray | 2.0 Å | A=329-430 |
| 2PXV | X-ray | 2.0 Å | A=329-430 |
| 7O9I | X-ray | 2.49 Å | A=3-299 |
| 2PXL | X-ray | 2.5 Å | A=329-430 |
| 2PXP | X-ray | 2.5 Å | A=329-430 |
| 2PXQ | X-ray | 2.5 Å | A=329-430 |
| 2PXT | X-ray | 2.5 Å | A=329-430 |
| 2PXU | X-ray | 2.5 Å | A=329-430 |
| 4C7O | X-ray | 2.6 Å | A/C=1-298 |
| 7O9G | X-ray | 2.8 Å | A=2-299 |
| 5GAD | EM | 3.7 Å | i=4-434 |
| 5GAG | EM | 3.8 Å | i=4-434 |
| 5GAH | EM | 3.8 Å | i=1-434 |
Showing 20 of 26 experimental structures (best resolution first).
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