Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN (WRN) is a 1432-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q14191.
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The mean pLDDT of this model is 68.6 (low 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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 28% |
| 70 to 90 | Confident: backbone generally right | 33% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 32% |
What pLDDT means and how to read it
Multifunctional enzyme that has magnesium and ATP-dependent 3'-5' DNA-helicase activity on partially duplex substrates (PubMed:9224595, PubMed:9288107, PubMed:9611231). Also has 3'->5' exonuclease activity towards double-stranded (ds)DNA with a 5'-overhang (PubMed:11863428). Has no nuclease activity towards single-stranded (ss)DNA or blunt-ended dsDNA (PubMed:11863428). Helicase activity is most efficient with (d)ATP, but (d)CTP will substitute with reduced efficiency; strand displacement is enhanced by single-strand binding-protein (heterotrimeric replication protein A complex, RPA1, RPA2, RPA3) (PubMed:9611231). Binds preferentially to DNA substrates containing alternate secondary…
Monomer, and homooligomer (PubMed:11863428, PubMed:18596042, PubMed:20159463). May exist as homodimer, homotrimer, homotetramer and/or homohexamer (PubMed:11863428, PubMed:18596042, PubMed:20159463). Homotetramer, or homohexamer, when bound to DNA (PubMed:11863428, PubMed:18596042, PubMed:20159463). Interacts via its N-terminal domain with WRNIP1 (By similarity). Interacts with EXO1, PCNA and…
Nucleus, nucleolus, Nucleus, Nucleus, nucleoplasm, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7GQU | X-ray | 1.54 Å | A=517-945 |
| 9OWB | X-ray | 1.56 Å | A/B/C/D=500-942 |
| 7GQS | X-ray | 1.57 Å | A=517-945 |
| 9MJU | X-ray | 1.58 Å | A=500-942 |
| 7XUT | X-ray | 1.6 Å | A/B=435-451 |
| 8PFP | X-ray | 1.6 Å | A=517-945 |
| 9MJY | X-ray | 1.63 Å | A=500-942 |
| 9OG8 | X-ray | 1.66 Å | A=526-946 |
| 9OWC | X-ray | 1.67 Å | A=500-942 |
| 9MJZ | X-ray | 1.7 Å | A=500-942 |
| 9MJT | X-ray | 1.73 Å | A=500-942 |
| 9MJX | X-ray | 1.73 Å | A=500-942 |
| 8PFL | X-ray | 1.8 Å | A=517-945 |
| 9MJS | X-ray | 1.84 Å | A=500-942 |
| 8YLE | X-ray | 1.86 Å | A=517-945 |
| 9MK0 | X-ray | 1.89 Å | A=500-942 |
| 3AAF | X-ray | 1.9 Å | A/B=949-1079 |
| 8PFO | X-ray | 1.9 Å | A=517-945 |
| 6TYV | X-ray | 1.93 Å | B=8-23 |
| 9OWD | X-ray | 1.96 Å | A=500-942 |
Showing 20 of 42 experimental structures (best resolution first).
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