Q9UBF6: RING-box protein 2 (RNF7)

RING-box protein 2 (RNF7) is a 113-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UBF6.

Gene
RNF7
Organism
Homo sapiens
Length
113 residues
Mean pLDDT
81.8
Model
AF-Q9UBF6-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.8 (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 accurate57%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution14%
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:21980433, PubMed:33268465, PubMed:38418882, PubMed:38574733, PubMed:35512830, PubMed:40440427, PubMed:40963025). It is thereby involved in various biological processes, such as cell cycle progression, signal transduction and transcription (PubMed:21980433, PubMed:33268465, PubMed:38418882, PubMed:38574733). The functional specificity of the E3 ubiquitin-protein ligase ECS complexes depend on the variable SOCS box-containing substrate recognition component (PubMed:21980433, PubMed:33268465).…

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:10230407, PubMed:21980433, PubMed:24337577, PubMed:25505247, PubMed:27910872, PubMed:31387940, PubMed:33268465,…

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9SDXEM2.97 ÅR=1-113
9SDYEM3.06 ÅR=1-113
7ONIEM3.4 ÅR=5-113
9EG1EM3.52 ÅK=1-113
9OMAEM4.14 ÅC=1-113
2ECLNMRA=40-113

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