Q14181: DNA polymerase alpha subunit B (POLA2)

DNA polymerase alpha subunit B (POLA2) is a 598-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q14181.

Gene
POLA2
Organism
Homo sapiens
Length
598 residues
Mean pLDDT
84.8
Model
AF-Q14181-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.8 (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 accurate64%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Accessory subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis (PubMed:9705292). During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, an accessory subunit POLA2 and two primase subunits, the catalytic subunit PRIM1 and the regulatory subunit PRIM2) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1 (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerizing short RNA primers on both leading and lagging strands (By similarity). These…

Subunit structure

Component of the alpha DNA polymerase complex (also known as the alpha DNA polymerase-primase complex) consisting of four subunits: the catalytic subunit POLA1, the regulatory subunit POLA2, and primase complex subunits PRIM1 and PRIM2 respectively (PubMed:26975377, PubMed:9705292). Within the complex, POLA1 directly interacts with PRIM2/p58 (By similarity)

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4Y97X-ray2.51 ÅA/C/E/G=1-598
8VY3EM2.98 ÅD=155-598
8QJ7EM3.07 ÅB=1-598
9C8VEM3.39 ÅD=155-598
8B9DEM3.4 ÅA=1-598
8D0BEM3.43 ÅG=143-598
8D9DEM3.59 ÅD=155-598
5EXRX-ray3.6 ÅD/H=2-598
7OPLEM4.12 ÅB=149-598
8D0KEM4.27 ÅG=2-598
7U5CEM4.6 ÅD=1-598
4E2IX-ray5.0 Å1/2/3/4/5/6/7/8/9/U/W=1-78
2KEBNMRA=1-78

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