Q9Y253: DNA polymerase eta (POLH)

DNA polymerase eta (POLH) is a 713-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y253.

Gene
POLH
Organism
Homo sapiens
Length
713 residues
Mean pLDDT
76.9
Model
AF-Q9Y253-F1 v6
Model created
1 Aug 2025
PDB structures
241

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 76.9 (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 accurate61%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions29%

What pLDDT means and how to read it

Function

DNA polymerase specifically involved in the DNA repair by translesion synthesis (TLS) (PubMed:10385124, PubMed:11743006, PubMed:16357261, PubMed:20388628, PubMed:24449906, PubMed:24553286, PubMed:38212351). Due to low processivity on both damaged and normal DNA, cooperates with the heterotetrameric (REV3L, REV7, POLD2 and POLD3) POLZ complex for complete bypass of DNA lesions. Inserts one or 2 nucleotide(s) opposite the lesion, the primer is further extended by the tetrameric POLZ complex. In the case of 1,2-intrastrand d(GpG)-cisplatin cross-link, inserts dCTP opposite the 3' guanine (PubMed:24449906). Particularly important for the repair of UV-induced pyrimidine dimers (PubMed:10385124,…

Subunit structure

Interacts with REV1 (via C-terminal domain) (PubMed:22691049). Interacts with monoubiquitinated PCNA, but not unmodified PCNA (PubMed:15149598). Interacts with POLI; this interaction targets POLI to the replication machinery (PubMed:12606586). Interacts with PALB2 and BRCA2; the interactions are direct and are required to sustain the recruitment of POLH at blocked replication forks and to…

Subcellular location

Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7M7NX-ray1.31 ÅA=1-432
5KFZX-ray1.44 ÅA=1-432
5KFNX-ray1.45 ÅA=1-432
5KFSX-ray1.46 ÅA=1-432
7M7MX-ray1.46 ÅA=1-432
7M7TX-ray1.46 ÅA=1-432
7M84X-ray1.47 ÅA=1-432
7U7LX-ray1.47 ÅA=1-432
4ECQX-ray1.5 ÅA=1-432
5KFCX-ray1.5 ÅA=1-432
5KFAX-ray1.51 ÅA=1-432
4ECVX-ray1.52 ÅA=1-432
4ED8X-ray1.52 ÅA=1-432
5KFOX-ray1.52 ÅA=1-432
5KFTX-ray1.52 ÅA=1-432
5KFXX-ray1.52 ÅA=1-432
7U74X-ray1.52 ÅA=1-432
8V7GX-ray1.52 ÅA=1-432
7U72X-ray1.53 ÅA=1-432
7U7UX-ray1.54 ÅA=1-432

Showing 20 of 241 experimental structures (best resolution first).

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.