DNA repair protein XRCC4 (XRCC4) is a 336-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13426.
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The mean pLDDT of this model is 74.8 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 56% |
| 70 to 90 | Confident: backbone generally right | 5% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 32% |
What pLDDT means and how to read it
DNA non-homologous end joining (NHEJ) core factor, required for double-strand break repair and V(D)J recombination (PubMed:10757784, PubMed:10854421, PubMed:12517771, PubMed:16412978, PubMed:17124166, PubMed:17290226, PubMed:22228831, PubMed:25597996, PubMed:25742519, PubMed:25934149, PubMed:26100018, PubMed:26774286, PubMed:8548796). Acts as a scaffold protein that regulates recruitment of other proteins to DNA double-strand breaks (DSBs) (PubMed:15385968, PubMed:20852255, PubMed:26774286, PubMed:27437582). Associates with NHEJ1/XLF to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired (PubMed:21768349,…
Homodimer and homotetramer in solution (PubMed:11080143, PubMed:25574025, PubMed:25670504, PubMed:25941166, PubMed:31548606, PubMed:17567543). Interacts with NHEJ1/XLF; the interaction is direct and is mediated via a head-to-head interaction between N-terminal head regions (PubMed:16439205, PubMed:17567543, PubMed:18158905, PubMed:20558749, PubMed:21768349, PubMed:21775435, PubMed:21936820,…
Nucleus, Chromosome, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5E50 | X-ray | 1.38 Å | C/D=228-236 |
| 7M3P | X-ray | 2.0 Å | A/B=2-132 |
| 3MUD | X-ray | 2.2 Å | A/B=2-135 |
| 1IK9 | X-ray | 2.3 Å | A/B=1-213 |
| 5CHX | X-ray | 2.3 Å | A/B=2-143 |
| 5CJ0 | X-ray | 2.3 Å | A/B=2-143 |
| 4XA4 | X-ray | 2.33 Å | A/B=2-147 |
| 3II6 | X-ray | 2.4 Å | A/B/C/D=1-203 |
| 5WJ7 | X-ray | 2.5 Å | A/B=2-132 |
| 6ABO | X-ray | 2.65 Å | A=1-213 |
| 1FU1 | X-ray | 2.7 Å | A/B=1-203 |
| 9CQ3 | EM | 2.8 Å | D/E/d/e=1-336 |
| 9N81 | EM | 2.8 Å | D/E/d/e=1-336 |
| 5CJ4 | X-ray | 3.1 Å | A/B/C/D=2-145 |
| 9CQ6 | EM | 3.1 Å | D/E/d/e=1-336 |
| 9N83 | EM | 3.1 Å | D/E/d/e=1-336 |
| 9N82 | EM | 3.3 Å | D/E/d/e=1-336 |
| 9CQC | EM | 3.4 Å | D/E/d/e=1-336 |
| 5WLZ | X-ray | 3.5 Å | A/B/C/D=2-132 |
| 3RWR | X-ray | 3.94 Å | A/B/F/G/J/K/N/P/R/U/V/Y=1-157 |
Showing 20 of 35 experimental structures (best resolution first).
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