P08839: Phosphoenolpyruvate-protein phosphotransferase (ptsI)

Phosphoenolpyruvate-protein phosphotransferase (ptsI) is a 575-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P08839.

Gene
ptsI
Organism
Escherichia coli (strain K12)
Length
575 residues
Mean pLDDT
90.3
Model
AF-P08839-F1 v6
Model created
1 Aug 2025
PDB structures
19

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 90.3 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate61%
70 to 90Confident: backbone generally right36%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr) (PubMed:12705838, PubMed:17053069, PubMed:7876255). Can also use (Z)-3-fluoro-PEP (ZFPEP), (Z)-3-methyl-PEP (ZMePEP), (Z)-3-chloro-PEP (ZClPEP) and (E)-3-chloro-PEP (EClPEP) as alternative phosphoryl donors (PubMed:12705838)

Subunit structure

Homodimer (PubMed:12705838, PubMed:17053069). Interacts with the pole-localizer protein TmaR (PubMed:33376208). Binding to TmaR is reversible as long as TmaR can get phosphorylated, whereas binding to non-phosphorylated TmaR is very strong and shifts the equilibrium toward binding (PubMed:33376208)

Subcellular location

Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6V9KX-ray1.9 ÅA/B=261-575
1ZYMX-ray2.5 ÅA/B=1-258
2HWGX-ray2.7 ÅA/B=1-575
6VU0X-ray3.5 ÅA/B=261-575
1EZANMRA=1-258
1EZBNMRA=1-258
1EZCNMRA=1-258
1EZDNMRA=1-258
2EZANMRA=1-258
2EZBNMRA=1-258
2EZCNMRA=1-258
2KX9OtherA/B=1-573
2L5HOtherA/B=1-573
2MP0NMRA=1-258
2N5TOtherA/B=1-575
2XDFOtherA/B=1-573
3EZANMRA=1-249
3EZBNMRA=1-259
3EZENMRA=1-258

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.