Q9WTZ1: RING-box protein 2 (Rnf7)

RING-box protein 2 (Rnf7) is a 113-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9WTZ1.

Gene
Rnf7
Organism
Mus musculus
Length
113 residues
Mean pLDDT
82.6
Model
AF-Q9WTZ1-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 82.6 (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 accurate62%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Catalytic component of multiple cullin-5-RING E3 ubiquitin-protein ligase complexes (ECS complexes), which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:22118770, PubMed:24210661, PubMed:29361558). It is thereby involved in various biological processes, such as cell cycle progression, signal transduction and transcription (PubMed:22118770, PubMed:24210661, PubMed:29361558). The functional specificity of the E3 ubiquitin-protein ligase ECS complexes depend on the variable SOCS box-containing substrate recognition component (PubMed:24210661). Within ECS complexes, RNF7/RBX2 recruits the E2 ubiquitination enzyme to the complex via its RING-type…

Subunit structure

Catalytic component of multiple cullin-5-RING E3 ubiquitin-protein ligase complexes (ECS complexes, also named CRL5 complexes) composed of CUL5, Elongin BC (ELOB and ELOC), RNF7/RBX2 and a variable SOCS box domain-containing protein as substrate-specific recognition component (PubMed:24210661, PubMed:32513959). Also interacts (with lower preference) with CUL1, CUL2, CUL3, CUL4A and CUL4B;…

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6V9IEM5.2 ÅR=1-113
9OMFEM9.72 ÅC=1-113

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