A0A0H2USC0: E3 ubiquitin-protein ligase IpaH2.5 (ipaH2.5)

E3 ubiquitin-protein ligase IpaH2.5 (ipaH2.5) is a 563-residue protein from Shigella flexneri. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: A0A0H2USC0.

Gene
ipaH2.5
Organism
Shigella flexneri
Length
563 residues
Mean pLDDT
85.5
Model
AF-A0A0H2USC0-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.5 (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 accurate55%
70 to 90Confident: backbone generally right33%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions7%

What pLDDT means and how to read it

Function

E3 ubiquitin-protein ligase effector that inhibits host cell innate immunity during bacterial infection by catalyzing 'Lys-48'-linked polyubiquitination and subsequent degradation of host RNF31/HOIP and RNF213 (PubMed:27572974, PubMed:36610722, PubMed:40205224). Host RNF31/HOIP is the catalytic component of the LUBAC complex, which conjugates linear ('Met-1'-linked) polyubiquitin chains at the surface of bacteria invading the host cytosol to form the ubiquitin coat surrounding bacteria (PubMed:27572974). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:27572974)

Subunit structure

Interacts with human RBCK1/HOIL-1 and RNF31/HOIP components of the LUBAC complex

Subcellular location

Secreted, Host cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7YA8X-ray3.4 ÅA/B=36-274
9G09EM3.4 ÅB=1-563

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