O95376: E3 ubiquitin-protein ligase ARIH2 (ARIH2)

E3 ubiquitin-protein ligase ARIH2 (ARIH2) is a 493-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O95376.

Gene
ARIH2
Organism
Homo sapiens
Length
493 residues
Mean pLDDT
86.5
Model
AF-O95376-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.5 (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 accurate75%
70 to 90Confident: backbone generally right11%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:16118314, PubMed:17646546, PubMed:19340006, PubMed:24076655, PubMed:33268465, PubMed:34518685, PubMed:38418882). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-5-RING ubiquitin ligase complex (ECS complex, also named CRL5 complex) and initiating ubiquitination of ECS substrates: associates with ECS complex and specifically mediates addition of the first ubiquitin on ECS targets (PubMed:33268465, PubMed:34518685, PubMed:38418882). The initial ubiquitin is then elongated (PubMed:33268465). E3 ubiquitin-protein ligase…

Subunit structure

Interacts with (neddylated) CUL5; promoting association with cullin-5-RING ubiquitin ligase complexes (ECS complexes) (PubMed:24076655, PubMed:33268465). Does not interact with other neddylated cullins (CUL1, CUL2, CUL3, CUL4A or CUL4B) (PubMed:24076655). Interacts (via RING-type zinc finger 1) with UBE2L3 (PubMed:16118314, PubMed:19340006, PubMed:24076655). Interacts (via RING-type zinc finger…

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7OD1X-ray2.45 ÅA/B=1-493
9SDXEM2.97 ÅH=1-493
9SDYEM3.06 ÅH=1-493
7ONIEM3.4 ÅH=1-493

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