Factor H binding protein (fhbP) is a 274-residue protein from Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9JXV4.
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The mean pLDDT of this model is 89.6 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 82% |
| 70 to 90 | Confident: backbone generally right | 7% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 11% |
What pLDDT means and how to read it
A bacterial surface lipoprotein that binds host (human) complement factor H (fH, gene CFH), binding contributes to the avoidance of complement-mediated lysis by N.meningitidis. Binding of fH to the bacteria surface is independent of bacterial sialic acid moieties (PubMed:16751403). fH binding affinity is high enough that it may sequester plasma fH, depleting its circulating levels and de-regulating complement in the host (Probable). This protein induces high levels of bactericidal antibodies in mice (PubMed:12642606, PubMed:15039331, PubMed:15664958, PubMed:21753121, PubMed:23133374)
Binds to host factor H (fH from human) (PubMed:16751403, PubMed:16785547, PubMed:19225461, PubMed:23133374). Both fHbp beta-barrels contact Sushi domains 6 and 7 in fH (also called complement control protein domains, CCP). This interaction probably mimics the normal (carbohydrate-dependent) mode of fH recruitment, regulating fH activity. Sucrose octasulphate inhibits the fHbp-fH interaction…
Cell outer membrane, Secreted, Extracellular vesicle, bacterial extracellular vesicle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8UP2 | X-ray | 1.6 Å | C/F=27-274 |
| 5NQZ | X-ray | 1.63 Å | A/B=27-274 |
| 7LCV | X-ray | 1.7 Å | C=20-274 |
| 2YPV | X-ray | 1.8 Å | A=23-274 |
| 2Y7S | X-ray | 1.9 Å | A/B=27-274 |
| 7KET | X-ray | 2.0 Å | C=20-274 |
| 5O14 | X-ray | 2.19 Å | A/B=27-274 |
| 2W80 | X-ray | 2.35 Å | C/D/F/H=25-274 |
| 2W81 | X-ray | 2.35 Å | C/D/F=25-274 |
| 4AYD | X-ray | 2.4 Å | C/D/F=27-274 |
| 6XZW | X-ray | 2.4 Å | D=27-274 |
| 4AYE | X-ray | 2.8 Å | C/D/F=27-274 |
| 7SBZ | X-ray | 2.9 Å | C/D=27-274 |
| 5T5F | X-ray | 2.98 Å | A=23-274 |
| 5NQX | X-ray | 3.66 Å | A/B/C/D/E=26-247, A/B/C/D/E=249-274 |
| 1YS5 | NMR | A=120-274 |
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