Q9BYM8: RanBP-type and C3HC4-type zinc finger-containing protein 1 (RBCK1)

RanBP-type and C3HC4-type zinc finger-containing protein 1 (RBCK1) is a 510-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BYM8.

Gene
RBCK1
Organism
Homo sapiens
Length
510 residues
Mean pLDDT
84.0
Model
AF-Q9BYM8-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.0 (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 accurate44%
70 to 90Confident: backbone generally right45%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions8%

What pLDDT means and how to read it

Function

E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates (PubMed:12629548, PubMed:17449468, PubMed:18711448). Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination (PubMed:12629548). Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome (PubMed:17449468, PubMed:18711448). Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (PubMed:17006537, PubMed:19136968, PubMed:21455173,…

Subunit structure

Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31 (PubMed:17006537, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22430200, PubMed:28481331). LUBAC has a MW of approximately 600 kDa suggesting a heteromultimeric assembly of its subunits (PubMed:17006537, PubMed:21455173, PubMed:21455180, PubMed:21455181). Interacts…

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8K6QX-ray1.59 ÅA/B/C/D=1-51
9EGWX-ray1.78 ÅA/B=425-510
7YUJX-ray1.86 ÅA/B=365-510
7V8EX-ray1.9 ÅC/D=53-135
9EGVX-ray2.0 ÅA/B=425-510
8BVLX-ray2.24 ÅA/B=368-510
7YUIX-ray2.6 ÅB=195-424
4DBGX-ray2.71 ÅA=37-137
8EAZX-ray3.08 ÅA/B=232-510
2CRCNMRA=194-232
2LGYNMRA=51-139

More AlphaFold highlights

About this viewer

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