P62878: E3 ubiquitin-protein ligase RBX1 (Rbx1)

E3 ubiquitin-protein ligase RBX1 (Rbx1) is a 108-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62878.

Gene
Rbx1
Organism
Mus musculus
Length
108 residues
Mean pLDDT
78.5
Model
AF-P62878-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 78.5 (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 accurate28%
70 to 90Confident: backbone generally right44%
50 to 70Low: treat with caution19%
Below 50Very low: often disordered regions8%

What pLDDT means and how to read it

Function

E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair (PubMed:22118460, PubMed:33590678, PubMed:35978186). CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets (By similarity). The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components…

Subunit structure

Component of multiple Cul1-RING E3 ubiquitin-protein ligase complexes commonly known as SCF (SKP1-CUL1-F-box) complexes, consisting of CUL1, SKP1, RBX1 and a variable F-box domain-containing protein (By similarity). Part of a SCF(SKP2) complex consisting of CUL1, RBX1, SKP1 and SKP2 (By similarity). Part of a SCF(FBXO3) complex consisting of CUL1, FBXO3, RBX1 and SKP1; this complex interacts…

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7OPCEM3.0 Åf=1-108
7OPDEM3.0 Åf=1-108
4A0CX-ray3.8 ÅD/F=12-108
4A0KX-ray5.93 ÅB=12-108
4A0LX-ray7.4 ÅF/I=12-108

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