O15205: Ubiquitin D (UBD)

Ubiquitin D (UBD) is a 165-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O15205.

Gene
UBD
Organism
Homo sapiens
Length
165 residues
Mean pLDDT
85.0
Model
AF-O15205-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.0 (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 accurate39%
70 to 90Confident: backbone generally right49%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Ubiquitin-like protein modifier which can be covalently attached to target proteins and subsequently leads to their degradation by the 26S proteasome, in a NUB1-dependent manner (PubMed:15831455, PubMed:16707496, PubMed:19166848). Conjugation to the target protein is activated by UBA6 via adenylation of its C-terminal glycine (PubMed:17889673, PubMed:35970836). Promotes the expression of the proteasome subunit beta type-9 (PSMB9/LMP2). Regulates TNF-induced and LPS-mediated activation of the central mediator of innate immunity NF-kappa-B by promoting TNF-mediated proteasomal degradation of ubiquitinated-I-kappa-B-alpha (PubMed:19959714). Required for TNF-induced p65 nuclear translocation…

Subunit structure

Interacts directly with the 26S proteasome (PubMed:16707496). Interacts with NUB1; this interaction facilitates the linking of UBD-conjugated target protein to the proteasome complex and accelerates its own degradation and that of its conjugates (PubMed:14757770, PubMed:16707496, PubMed:25422469). Interacts (via ubiquitin-like 1 domain) with the spindle checkpoint protein MAD2L1 during mitosis…

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6GF1X-ray1.93 ÅA/B/C=10-86
9E8OEM3.1 Åg=1-165
7PYVX-ray3.27 ÅC=7-165
2MBENMRA=8-82
6GF2NMRA=85-165

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