P50456: DNA-binding transcriptional repressor Mlc (mlc)

DNA-binding transcriptional repressor Mlc (mlc) is a 406-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P50456.

Gene
mlc
Organism
Escherichia coli (strain K12)
Length
406 residues
Mean pLDDT
93.1
Model
AF-P50456-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 93.1 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate86%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions2%

What pLDDT means and how to read it

Function

Global regulator of carbohydrate metabolism (PubMed:10464268, PubMed:11361067, PubMed:11934616, PubMed:9484892, PubMed:9484893, PubMed:9781886). Represses the expression of several genes involved in sugar transport and utilization, in particular phosphoenolpyruvate-carbohydrate phosphotransferase system (PTS) genes (PubMed:10464268, PubMed:9484892, PubMed:9484893, PubMed:9781886). Represses expression of ptsG (EIICB(Glc)), which encodes the PTS system glucose-specific EIICB component (PubMed:9781886). Also represses the expression of the manXYZ operon, encoding the mannose-specific PTS system, expression of malT, encoding the transcriptional activator of the maltose regulon, and expression…

Subunit structure

Homodimer (PubMed:15929984). Homotetramer (PubMed:12529317, PubMed:15929984, PubMed:16510988, PubMed:18319344). There is probably an equilibrium between the dimeric and the tetrameric form (PubMed:15929984). Interacts with dephosphorylated PtsG (PubMed:11032803, PubMed:11157755, PubMed:12529317, PubMed:18319344). Mlc and PtsG EIIB domain form a complex with the 1:1 stoichiometry…

Subcellular location

Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1Z6RX-ray2.7 ÅA/B/C/D=1-406
3BP8X-ray2.85 ÅA/B=1-406

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