P53044: Ubiquitin fusion degradation protein 1 (UFD1)

Ubiquitin fusion degradation protein 1 (UFD1) is a 361-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P53044.

Gene
UFD1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
361 residues
Mean pLDDT
69.9
Model
AF-P53044-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 69.9 (low 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 accurate7%
70 to 90Confident: backbone generally right44%
50 to 70Low: treat with caution35%
Below 50Very low: often disordered regions15%

What pLDDT means and how to read it

Function

Functions at a post-ubiquitation step in the ubiquitin fusion degradation (UFD) pathway. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway. Required for the proteasome-dependent processing/activation of MGA2 and SPT23 transcription factors leading to the subsequent expression of OLE1. Has an additional role in the turnover of OLE1 where it targets ubiquitinated OLE1 and other proteins to the ERAD

Subunit structure

Component of the heterotrimeric CDC48-NPL4-UFD1 ATPase complex (PubMed:16873066). The CDC48-NPL4-UFD1 ATPase complex interacts with the HRD1 ubiquitin ligase complex composed of the E3 ligase HRD1, its cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and CDC48-binding protein UBX2 (PubMed:16873066). Interaction between the complexes is mediated by interaction between…

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6JWJX-ray1.58 ÅC=288-305
8DAREM3.0 ÅH=1-361
8DASEM3.5 ÅH=1-361
8DAVEM3.5 ÅH=1-361
8DAWEM3.6 ÅH=1-361
8DAUEM3.7 ÅH=1-361
8DATEM3.8 ÅH=1-361
1ZC1NMRA=1-208

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