O00206: Toll-like receptor 4 (TLR4)

Toll-like receptor 4 (TLR4) is a 839-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O00206.

Gene
TLR4
Organism
Homo sapiens
Length
839 residues
Mean pLDDT
89.2
Model
AF-O00206-F1 v6
Model created
1 Aug 2025
PDB structures
15

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.2 (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 accurate72%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Transmembrane receptor that functions as a pattern recognition receptor recognizing pathogen- and damage-associated molecular patterns (PAMPs and DAMPs) to induce innate immune responses via downstream signaling pathways (PubMed:10835634, PubMed:15809303, PubMed:16622205, PubMed:17292937, PubMed:17478729, PubMed:20037584, PubMed:20711192, PubMed:23880187, PubMed:27022195, PubMed:29038465, PubMed:17803912, PubMed:15852007). At the plasma membrane, cooperates with LY96 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:27022195). Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate, and Ni(2+)…

Subunit structure

Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4 (PubMed:11274165). Binding to bacterial LPS leads to homodimerization. Interacts with LY96 via the extracellular domain (PubMed:17803912, PubMed:19252480). Interacts with MYD88 (PubMed:36232715). Interacts (via TIR domains) with TIRAP (By similarity). Interacts with TICAM2…

Subcellular location

Cell membrane, Early endosome, Cell projection, ruffle

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2Z62X-ray1.7 ÅA=27-228
2Z66X-ray1.9 ÅA/B/C/D=384-627
2Z63X-ray2.0 ÅA=27-530
8WO1EM2.24 ÅA/B=27-631
3UL7X-ray2.37 ÅA=28-226
4G8AX-ray2.4 ÅA/B=23-629
3UL9X-ray2.45 ÅA=28-228
3UL8X-ray2.5 ÅA=27-228
2Z65X-ray2.7 ÅA/B=27-228
9J03EM2.7 ÅA/B=27-631
8WTAEM2.9 ÅA/B=27-631
3FXIX-ray3.1 ÅA/B=27-631
3ULAX-ray3.6 ÅA/C=27-228
5NAMNMRA=623-670
5NAONMRA=623-657

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