Q9UF56: F-box/LRR-repeat protein 17 (FBXL17)

F-box/LRR-repeat protein 17 (FBXL17) is a 701-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UF56.

Gene
FBXL17
Organism
Homo sapiens
Length
701 residues
Mean pLDDT
68.4
Model
AF-Q9UF56-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 68.4 (low 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 accurate47%
70 to 90Confident: backbone generally right6%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions43%

What pLDDT means and how to read it

Function

Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC) (PubMed:30190310). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteasome (PubMed:30190310). The ability of the SCF(FBXL17) complex to eliminate compromised BTB dimers is required for the differentiation and survival of neural crest and neuronal cells (By…

Subunit structure

Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXL17) composed of CUL1, SKP1, RBX1 and FBXL17 (PubMed:24035498). Interacts with BTB domain-containing proteins such as KLHL12, BCL6 and BACH1; specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition (PubMed:30190310). Interacts with…

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8UBTEM3.1 ÅC=310-701
6W66X-ray3.21 ÅB=310-701
8UAHEM3.3 ÅB=310-701
8UBVEM4.1 ÅB/H=310-701
8UBUEM4.6 ÅD/K=310-701
6WCQEM8.5 ÅB=310-701

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