P49005: DNA polymerase delta subunit 2 (POLD2)

DNA polymerase delta subunit 2 (POLD2) is a 469-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P49005.

Gene
POLD2
Organism
Homo sapiens
Length
469 residues
Mean pLDDT
89.1
Model
AF-P49005-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.1 (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 accurate74%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Accessory component of both the DNA polymerase delta complex and the DNA polymerase zeta complex (PubMed:17317665, PubMed:22801543, PubMed:24449906). As a component of the trimeric and tetrameric DNA polymerase delta complexes (Pol-delta3 and Pol-delta4, respectively), plays a role in high fidelity genome replication, including in lagging strand synthesis, and repair (PubMed:12403614, PubMed:16510448, PubMed:19074196, PubMed:20334433, PubMed:24035200). Pol-delta3 and Pol-delta4 are characterized by the absence or the presence of POLD4. They exhibit differences in catalytic activity. Most notably, Pol-delta3 shows higher proofreading activity than Pol-delta4 (PubMed:19074196,…

Subunit structure

Component of both the DNA polymerase delta and DNA polymerase zeta complexes (PubMed:17317665, PubMed:22801543, PubMed:24449906, PubMed:31449058). Component of the tetrameric DNA polymerase delta complex (Pol-delta4), which consists of POLD1/p125, POLD2/p50, POLD3/p66/p68 and POLD4/p12, with POLD1 bearing DNA polymerase and 3' to 5' proofreading exonuclease activities (PubMed:17317665,…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3E0JX-ray3.0 ÅA/C/E/G=1-469
6TNYEM3.08 ÅB=1-469
9EKBEM3.65 ÅB=1-469
6TNZEM4.05 ÅB=1-469
6S1MEM4.27 ÅB=1-469
6S1NEM4.86 ÅB=1-469
6S1OEM8.1 ÅB=1-469

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