Q93034: Cullin-5 (CUL5)

Cullin-5 (CUL5) is a 780-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q93034.

Gene
CUL5
Organism
Homo sapiens
Length
780 residues
Mean pLDDT
89.3
Model
AF-Q93034-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.3 (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 accurate70%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Core component of multiple cullin-5-RING E3 ubiquitin-protein ligase complexes (ECS complexes, also named CRL5 complexes), which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:11384984, PubMed:15601820, PubMed:21199876, PubMed:21980433, PubMed:23897481, PubMed:25505247, PubMed:27910872, PubMed:32200094, PubMed:33268465, PubMed:35512830, PubMed:38418882, PubMed:40963025). Acts a scaffold protein that contributes to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:11384984, PubMed:15601820, PubMed:33268465). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable…

Subunit structure

Component of multiple cullin-5-RING E3 ubiquitin-protein ligase complexes (ECS complexes, also named CRL5 complexes) formed of CUL5, Elongin BC (ELOB and ELOC), RNF7/RBX2 and a variable SOCS box domain-containing protein as substrate-specific recognition component (PubMed:11384984, PubMed:15601820, PubMed:16325183, PubMed:21119685, PubMed:27910872, PubMed:32513959, PubMed:33268465,…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3DPLX-ray2.6 ÅC=401-780
8EI2X-ray2.8 ÅA=1-386
9SDXEM2.97 ÅC=1-780
3DQVX-ray3.0 ÅC/D=401-780
4JGHX-ray3.0 ÅD=10-386
9SDYEM3.06 ÅC=1-780
8FVIEM3.24 Åx=11-320
4N9FX-ray3.3 Å3/9/C/I/O/U/V/f/l/r/w/x=12-321
7ONIEM3.4 ÅC=1-780
9EG1EM3.52 ÅJ=1-780
8FVJEM3.54 Å2/7=12-320
9OMAEM4.14 ÅB=1-780
6V9IEM5.2 ÅC=2-780
9OMFEM9.72 ÅB=1-780

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