P13051: Uracil-DNA glycosylase (UNG)

Uracil-DNA glycosylase (UNG) is a 313-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P13051.

Gene
UNG
Organism
Homo sapiens
Length
313 residues
Mean pLDDT
85.3
Model
AF-P13051-F1 v6
Model created
1 Aug 2025
PDB structures
24

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.3 (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 accurate72%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions16%

What pLDDT means and how to read it

Function

Uracil-DNA glycosylase that hydrolyzes the N-glycosidic bond between uracil and deoxyribose in single- and double-stranded DNA (ssDNA and dsDNA) to release a free uracil residue and form an abasic (apurinic/apyrimidinic; AP) site. Excises uracil residues arising as a result of misincorporation of dUMP residues by DNA polymerase during replication or due to spontaneous or enzymatic deamination of cytosine (PubMed:12958596, PubMed:15967827, PubMed:17101234, PubMed:22521144, PubMed:7671300, PubMed:8900285, PubMed:9016624, PubMed:9776759). Mediates error-free base excision repair (BER) of uracil at replication forks. According to the model, it is recruited by PCNA to S-phase replication forks…

Subunit structure

Monomer

Subcellular location

Mitochondrion, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3FCIX-ray1.27 ÅA=94-313
2HXMX-ray1.3 ÅA=94-313
3TKBX-ray1.5 ÅA=94-313
1AKZX-ray1.57 ÅA=94-313
3FCKX-ray1.64 ÅB=94-313
3FCLX-ray1.7 ÅA/B=94-313
9LNQX-ray1.74 ÅE=94-312
9LNPX-ray1.76 ÅE=94-313
1EMHX-ray1.8 ÅA=91-313
6VBAX-ray1.8 ÅA=94-313
3FCFX-ray1.84 ÅA=94-313
1Q3FX-ray1.9 ÅA=94-313
1SSPX-ray1.9 ÅE=94-313
1UGHX-ray1.9 ÅE=94-313
1YUOX-ray1.95 ÅA=91-313
1EMJX-ray2.0 ÅA=91-313
2OYTX-ray2.0 ÅA=94-313
2SSPX-ray2.25 ÅE=94-313
5AYRX-ray2.4 ÅA/C=94-313
2OXMX-ray2.5 ÅA=94-313

Showing 20 of 24 experimental structures (best resolution first).

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About this viewer

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