Q96LW4: DNA-directed primase/polymerase protein (PRIMPOL)

DNA-directed primase/polymerase protein (PRIMPOL) is a 560-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96LW4.

Gene
PRIMPOL
Organism
Homo sapiens
Length
560 residues
Mean pLDDT
74.0
Model
AF-Q96LW4-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.0 (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 accurate52%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions25%

What pLDDT means and how to read it

Function

DNA primase and DNA polymerase required to tolerate replication-stalling lesions by bypassing them (PubMed:24126761, PubMed:24207056, PubMed:24240614, PubMed:24267451, PubMed:24682820, PubMed:25255211, PubMed:25262353, PubMed:25550423, PubMed:25746449, PubMed:27989484, PubMed:28534480, PubMed:29608762, PubMed:30889508, PubMed:31676232). Required to facilitate mitochondrial and nuclear replication fork progression by initiating de novo DNA synthesis using dNTPs and acting as an error-prone DNA polymerase able to bypass certain DNA lesions (PubMed:24126761, PubMed:24207056, PubMed:24240614, PubMed:24267451, PubMed:24682820, PubMed:25255211, PubMed:25262353, PubMed:25550423, PubMed:25746449,…

Subunit structure

Interacts with RPA1; leading to recruitment to chromatin and stimulate DNA primase activity (PubMed:24126761, PubMed:25550423, PubMed:28396594, PubMed:28534480). Interacts with SSBP1 (PubMed:25550423). Interacts with POLDIP2; leading to enhance DNA polymerase activity (PubMed:26984527)

Subcellular location

Nucleus, Mitochondrion matrix, Chromosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5N8AX-ray1.28 ÅX=480-560
5N85X-ray2.0 ÅB=514-528
7JLGX-ray2.07 ÅA/B=1-354
7JL8X-ray2.1 ÅA/B=1-354
5L2XX-ray2.2 ÅA/B=1-353
7JKLX-ray2.38 ÅA/B=1-354
7JKPX-ray2.59 ÅA/B=1-354
7JK1X-ray2.62 ÅA/B=1-354

More AlphaFold highlights

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