Q9HCU8: DNA polymerase delta subunit 4 (POLD4)

DNA polymerase delta subunit 4 (POLD4) is a 107-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9HCU8.

Gene
POLD4
Organism
Homo sapiens
Length
107 residues
Mean pLDDT
84.8
Model
AF-Q9HCU8-F1 v6
Model created
1 Aug 2025
PDB structures
7

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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 accurate61%
70 to 90Confident: backbone generally right18%
50 to 70Low: treat with caution16%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

As a component of the tetrameric DNA polymerase delta complex (Pol-delta4), plays a role in high fidelity genome replication and repair. Within this complex, increases the rate of DNA synthesis and decreases fidelity by regulating POLD1 polymerase and proofreading 3' to 5' exonuclease activity (PubMed:16510448, PubMed:19074196, PubMed:20334433). Pol-delta4 participates in Okazaki fragment processing, through both the short flap pathway, as well as a nick translation system (PubMed:24035200). Under conditions of DNA replication stress, required for the repair of broken replication forks through break-induced replication (BIR), a mechanism that may induce segmental genomic duplications of up…

Subunit structure

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:16510448, PubMed:17317665, PubMed:22801543). Within this complex, directly interacts with POLD1 and POLD2 (PubMed:12403614, PubMed:16510448). Directly interacts with…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6HVOX-ray2.1 ÅD/E/F=1-19
6TNYEM3.08 ÅD=2-107
9EKBEM3.65 ÅD=1-107
6TNZEM4.05 ÅD=2-107
6S1MEM4.27 ÅD=2-107
6S1NEM4.86 ÅD=2-107
6S1OEM8.1 ÅD=2-107

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