P69776: Major outer membrane lipoprotein Lpp (lpp)

Major outer membrane lipoprotein Lpp (lpp) is a 78-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P69776.

Gene
lpp
Organism
Escherichia coli (strain K12)
Length
78 residues
Mean pLDDT
85.3
Model
AF-P69776-F1 v6
Model created
1 Aug 2025
PDB structures
15

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.3 (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 accurate59%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution28%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm (PubMed:29257832). The only protein known to be covalently linked to the peptidoglycan network (PGN) (PubMed:3013869, PubMed:4245367, PubMed:4261992). Also non-covalently binds the PGN (PubMed:3013869). The link between the cell outer membrane and PGN contributes to the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (PubMed:3013869, PubMed:4245367, PubMed:4261992, PubMed:4565677). The most abundant cellular protein in terms of copy…

Subunit structure

Homotrimer (PubMed:10843861, PubMed:3013869). Interacts with OmpA (PubMed:3013869). Has been isolated from outer membrane preparations as an approximately 87 kDa complex, suggesting it also forms larger complexes (PubMed:16079137). Seems to interact with TolB, Pal and TonB (PubMed:9701827). In pull-down experiments interacts with CedA (PubMed:28818726)

Subcellular location

Cell outer membrane, Secreted, cell wall

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1JCDX-ray1.3 ÅA/B/C=22-73
2GUVX-ray1.4 ÅA/B/C/D/E=22-77
1T8ZX-ray1.45 ÅA/B/C/D/E=22-74
1KFNX-ray1.65 ÅA=22-77
1JCCX-ray1.7 ÅA/B/C=22-77
2GUSX-ray1.75 ÅA=22-77
1EQ7X-ray1.9 ÅA=22-77
1KFMX-ray2.0 ÅA=22-77
9RLCEM2.8 ÅL=21-77
9RLDEM3.0 ÅL=21-77
7ARJEM3.2 ÅV=21-30
7ARLEM3.2 ÅV=21-30
7ARHEM3.3 ÅV=21-30
9GRCEM3.5 ÅV=21-30
7ARMEM3.6 ÅV=21-30

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