Q96SW2: Protein cereblon (CRBN)

Protein cereblon (CRBN) is a 442-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96SW2.

Gene
CRBN
Organism
Homo sapiens
Length
442 residues
Mean pLDDT
86.6
Model
AF-Q96SW2-F1 v6
Model created
1 Aug 2025
PDB structures
90

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.6 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate72%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions9%

What pLDDT means and how to read it

Function

Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2, ILF2, GLUL, IKZF1 and CSNK1A1 (PubMed:26990986, PubMed:33009960, PubMed:41565821). Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8 (PubMed:20223979, PubMed:24328678, PubMed:25043012, PubMed:25108355). Maintains presynaptic glutamate release and consequently cognitive functions, such as memory and learning, by negatively regulating large-conductance calcium-activated potassium (BK) channels in excitatory neurons…

Subunit structure

Component of a DCX (DDB1-CUL4-X-box) protein ligase complex, at least composed of CRBN, CUL4A, DDB1 and RBX1 (PubMed:25043012, PubMed:41565821). Interacts (via Lon N-terminal domain) with DDB1 (via WD40 beta-propellers A and C); the interaction is direct (PubMed:25043012, PubMed:25108355, PubMed:41565821). Interacts with IKZF1 and IKZF3; the interaction is direct and requires the presence of…

Subcellular location

Cytoplasm, Nucleus, Membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4M91X-ray1.1 ÅB=229-240
9CUOX-ray1.6 ÅA/B/C/D/E/F=319-427
9OHQX-ray1.6 ÅA/C/E/G=319-426
9DOMX-ray1.69 ÅA/C/E/G=319-426
7BQVX-ray1.8 ÅA=318-426
9O91X-ray1.86 ÅA/C/E/G=318-426
7BQUX-ray1.9 ÅA=318-426
9GAOX-ray1.95 ÅA/C=41-187, A/C=249-426
9FJXX-ray2.0 ÅB=40-442
8RQCX-ray2.15 ÅA/D=41-187, A/D=249-426
8RQ8X-ray2.19 ÅA=41-187, A=249-426
9OHRX-ray2.34 ÅA/C/E/G=319-426
9SFMX-ray2.39 ÅB=46-427
8TNQEM2.41 ÅB=1-442
9ODRX-ray2.42 ÅA/B/C/D=319-426
5FQDX-ray2.45 ÅB/E=41-442
8OIZX-ray2.5 ÅB=40-442
8RQAX-ray2.5 ÅA=41-187, A=249-426
8TNREM2.5 ÅB=1-442
9GY3X-ray2.5 ÅA/C=41-187, A/C=249-426

Showing 20 of 90 experimental structures (best resolution first).

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