Q13619: Cullin-4A (CUL4A)

Cullin-4A (CUL4A) is a 759-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13619.

Gene
CUL4A
Organism
Homo sapiens
Length
759 residues
Mean pLDDT
88.6
Model
AF-Q13619-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.6 (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 accurate73%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions5%

What pLDDT means and how to read it

Function

Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination of target proteins (PubMed:14578910, PubMed:14739464, PubMed:15448697, PubMed:15548678, PubMed:15811626, PubMed:16678110, PubMed:17041588, PubMed:24209620, PubMed:30166453, PubMed:33854232, PubMed:33854239). As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:14739464, PubMed:15448697, PubMed:15548678, PubMed:15811626, PubMed:16678110, PubMed:17041588, PubMed:24209620). The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit…

Subunit structure

Can self-associate (PubMed:17254749). Component of multiple DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes that seem to consist of DDB1, CUL4A or CUL4B, RBX1 and a variable substrate recognition component which seems to belong to a protein family described as DCAF (Ddb1- and Cul4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins (PubMed:12732143, PubMed:14578910,…

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7OPCEM3.0 Åe=1-759
7OPDEM3.0 Åe=1-759
2HYEX-ray3.1 ÅC=1-759
9EG8EM3.39 ÅJ=1-759
8B3IEM3.5 Åe=1-759
8B3GEM4.4 Åe=1-759
4A0KX-ray5.93 ÅA=38-759
7OKQEM8.4 ÅC/G/K/O=35-759

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