P62877: E3 ubiquitin-protein ligase RBX1 (RBX1)

E3 ubiquitin-protein ligase RBX1 (RBX1) is a 108-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62877.

Gene
RBX1
Organism
Homo sapiens
Length
108 residues
Mean pLDDT
79.3
Model
AF-P62877-F1 v6
Model created
1 Aug 2025
PDB structures
99

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.3 (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 accurate24%
70 to 90Confident: backbone generally right48%
50 to 70Low: treat with caution21%
Below 50Very low: often disordered regions7%

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:10230407, PubMed:10579999, PubMed:11961546, PubMed:15983046, PubMed:16678110, PubMed:19112177, PubMed:19679664, PubMed:22748924, PubMed:23455478, PubMed:27565346, PubMed:29769719, PubMed:32355176, PubMed:33417871, PubMed:37844242, PubMed:38326650, PubMed:39504960, PubMed:39667934, PubMed:38316879). CRLs complexes and ARIH1 collaborate in tandem to…

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 (PubMed:10230406, PubMed:11961546, PubMed:20596027, PubMed:22748924, PubMed:38326650, PubMed:39880951). Part of a SCF(SKP2) complex consisting of CUL1, RBX1, SKP1 and SKP2 (PubMed:10230406,…

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3DPLX-ray2.6 ÅR=5-108
7Z8REM2.7 ÅR=5-108
7Z8VEM2.7 ÅR=5-108
7PLOEM2.8 ÅT=1-108
7Z8BEM2.8 ÅR=1-108
8OR3EM2.9 ÅB=1-108
9QO4EM2.95 ÅJ=1-108
9EFQEM2.96 ÅK=1-108
1LDJX-ray3.0 ÅB=19-108
3DQVX-ray3.0 ÅR/Y=5-108
4F52X-ray3.0 ÅB/D=5-108
7Z8TEM3.0 ÅR=5-108
9EFVEM3.03 ÅK=1-108
1LDKX-ray3.1 ÅC=19-108
1U6GX-ray3.1 ÅB=1-108
2HYEX-ray3.1 ÅD=1-108
7ZBZEM3.1 ÅR=5-108
8OR0EM3.1 ÅB=1-108
4P5OX-ray3.11 ÅB/D=3-108
9XZJEM3.13 ÅR=1-108

Showing 20 of 99 experimental structures (best resolution first).

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