PTS system glucose-specific EIICB component (ptsG) is a 477-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P69786.
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The mean pLDDT of this model is 90.1 (very high 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 | 68% |
| 70 to 90 | Confident: backbone generally right | 27% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport (PubMed:10562420, PubMed:3129430). Also functions as a chemoreceptor monitoring the environment for changes in sugar concentration and an effector modulating the activity of the transcriptional repressor Mlc (PubMed:18319344). In the presence of glucose in the medium, the dephosphorylated form of PtsG can interact with Mlc, leading to sequestration of Mlc in the…
Homodimer (Probable) (PubMed:10562420, PubMed:12716891, PubMed:18319344). The dephosphorylated form interacts with the Mlc transcriptional repressor (PubMed:11032803, PubMed:11157755, PubMed:12529317, PubMed:18319344). Mlc and the EIIB domain form a complex with the 1:1 stoichiometry (PubMed:18319344)
Cell inner membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3BP3 | X-ray | 1.65 Å | A/B=396-477 |
| 9HNP | EM | 2.53 Å | A/B=1-477 |
| 8QSR | EM | 2.56 Å | A/B=1-477 |
| 3BP8 | X-ray | 2.85 Å | C/D=401-475 |
| 8QST | EM | 2.89 Å | A/B=1-477 |
| 1IBA | NMR | A=390-476 | |
| 1O2F | NMR | B=387-476 |
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