Q64339: Ubiquitin-like protein ISG15 (Isg15)

Ubiquitin-like protein ISG15 (Isg15) is a 161-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q64339.

Gene
Isg15
Organism
Mus musculus
Length
161 residues
Mean pLDDT
88.8
Model
AF-Q64339-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.8 (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 accurate65%
70 to 90Confident: backbone generally right30%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein. ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a lysine residue in the target protein. Its target proteins include SERPINA3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, TRIM25, STAT5A, MAPK1/ERK2 and globin. Isgylation of the viral sensor IFIH1/MDA5 promotes IFIH1/MDA5 oligomerization and triggers activation of innate immunity against a range of viruses, including coronaviruses, flaviviruses and picornaviruses. Can…

Subunit structure

Homodimer; disulfide-linked (By similarity). Interacts with, and is conjugated to its targets by the UBE1L (E1 enzyme) and UBE2E2 (E2 enzyme) (By similarity). Interacts with NEDD4 (By similarity). Interacts with PARP12; this interaction inhibits PINK1/Parkin-dependent mitophagy (By similarity)

Subcellular location

Cytoplasm, Secreted

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5CHWX-ray2.1 ÅA/B/C/D/E/F/G/H/I/J=1-155
5CHFX-ray2.3 ÅA/B/C/D/E=1-155
5TL7X-ray2.44 ÅA/C=78-155
5JZEX-ray2.47 ÅB/D=79-154
6J62X-ray2.49 ÅA=1-153
5CHVX-ray3.0 ÅC/D=1-155
6YVAX-ray3.18 ÅC=1-161
5TLAX-ray3.24 ÅA/B/C/D/E/F/G/H/I/J=1-150

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