P61077: Ubiquitin-conjugating enzyme E2 D3 (UBE2D3)

Ubiquitin-conjugating enzyme E2 D3 (UBE2D3) is a 147-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61077.

Gene
UBE2D3
Organism
Homo sapiens
Length
147 residues
Mean pLDDT
96.4
Model
AF-P61077-F1 v6
Model created
1 Aug 2025
PDB structures
45

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Model confidence (pLDDT)

The mean pLDDT of this model is 96.4 (very high 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 accurate97%
70 to 90Confident: backbone generally right3%
50 to 70Low: treat with caution0%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (PubMed:15247280, PubMed:15496420, PubMed:18284575, PubMed:20061386, PubMed:21532592, PubMed:28322253). In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination (PubMed:15247280, PubMed:15496420, PubMed:18284575, PubMed:20061386, PubMed:21532592). Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation (PubMed:20347421). Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin (PubMed:10329681). Ubiquitin chain…

Subunit structure

Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex; when Cullin is neddylated, the interaction between the E2 and the SCF complex is strengthened. Interacts with DAPK3. Interacts with BRCA1; the DNA damage checkpoint promotes the association with BRCA1 after ionizing radiation. Interacts non-covalently with ubiquitin. Interacts with E3 ubiquitin-protein ligase CBLC.…

Subcellular location

Cell membrane, Endosome membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5EGGX-ray1.76 ÅA=1-147
1X23X-ray1.85 ÅA/B/C/D=1-147
4S3OX-ray2.0 ÅA/D=2-147
8UQAX-ray2.05 ÅK=2-147
5IFRX-ray2.2 ÅA=2-147
8UQ9X-ray2.3 ÅA/a=2-147
8UQ8X-ray2.34 ÅA/a=2-147
3UGBX-ray2.35 ÅA=1-147
8AMSX-ray2.4 ÅA/B=1-147
8UQBX-ray2.48 ÅA=2-147
6T7FX-ray2.58 ÅB=2-147
8UQCX-ray2.61 ÅA=2-147
3RPGX-ray2.65 ÅA=2-147
4BVUX-ray2.7 ÅB=1-147
6CP0X-ray3.01 ÅB=1-147
9LPKEM3.03 ÅD/E=1-147
3L1ZX-ray3.17 ÅA=1-147
8SMXEM3.2 ÅL=1-147
8SMYEM3.2 ÅL=1-147
8SMZEM3.2 ÅL=1-147

Showing 20 of 45 experimental structures (best resolution first).

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