Q96HY6: DDRGK domain-containing protein 1 (DDRGK1)

DDRGK domain-containing protein 1 (DDRGK1) is a 314-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96HY6.

Gene
DDRGK1
Organism
Homo sapiens
Length
314 residues
Mean pLDDT
74.6
Model
AF-Q96HY6-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.6 (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 accurate39%
70 to 90Confident: backbone generally right27%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions21%

What pLDDT means and how to read it

Function

Component of the UFM1 ribosome E3 ligase (UREL) complex, a multiprotein complex that catalyzes ufmylation of endoplasmic reticulum-docked proteins (PubMed:30626644, PubMed:32160526, PubMed:35753586, PubMed:36121123, PubMed:36543799, PubMed:37595036, PubMed:37795761, PubMed:38383785, PubMed:38383789). The UREL complex plays a key role in ribosome recycling by mediating mono-ufmylation of the RPL26/uL24 subunit of the 60S ribosome following ribosome dissociation: ufmylation weakens the junction between post-termination 60S subunits and SEC61 translocons, promoting release and recycling of the large ribosomal subunit from the endoplasmic reticulum membrane (PubMed:38383785, PubMed:38383789).…

Subunit structure

Component of the UFM1 ribosome E3 ligase (UREL) complex, composed of UFL1, DDRGK1 and CDK5RAP3 (PubMed:20228063, PubMed:25219498, PubMed:32160526, PubMed:36121123, PubMed:36543799, PubMed:37595036, PubMed:38383785, PubMed:38383789). Interacts with (unphosphorylated) ERN1/IRE1-alpha; interaction is dependent on UFM1 and takes place in response to endoplasmic reticulum stress, regulating…

Subcellular location

Endoplasmic reticulum membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7W3NX-ray1.6 ÅA=194-202
8C0DX-ray2.56 ÅB/E=205-314
8OJ5EM2.9 ÅC=1-314
9GY4EM3.0 ÅC=1-314
8B9XX-ray3.07 ÅA/B=207-305
8OHDEM3.1 ÅC=1-314
8QFCEM3.2 ÅD=29-314
8OJ0EM3.3 ÅC=1-314

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