X-ray repair cross-complementing protein 5 (XRCC5) is a 732-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P13010.
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The mean pLDDT of this model is 83.1 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 57% |
| 70 to 90 | Confident: backbone generally right | 26% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
DNA-binding protein critical for the DNA damage response, specifically in repairing double-strand breaks (DSBs) via the classical non-homologous end joining (NHEJ) pathway. It forms a heterodimer with XRCC6 (Ku70), creating the Ku70:Ku80 heterodimer (Ku complex), which serves as a DNA end-binding complex. It primarily binds DSBs and recruits essential repair factors, assembling the core long-range NHEJ complex to facilitate the alignment and ligation of broken DNA ends (PubMed:11493912, PubMed:33854234, PubMed:34352203). This pathway ensures the rapid repair of cytotoxic and mutagenic DSBs and contributes to the generation of diversity in T-cell receptors and antibodies through mechanisms…
Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70; heterodimerization stabilizes XRCC5 protein (PubMed:11493912, PubMed:22442688, PubMed:25670504, PubMed:25941166, PubMed:35545041). Component of the core long-range non-homologous end joining (NHEJ) complex (also named DNA-PK complex) composed of PRKDC, LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF (PubMed:11493912, PubMed:22442688,…
Nucleus, Nucleus, nucleolus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3RZ9 | X-ray | 2.29 Å | B=559-571 |
| 8AG4 | EM | 2.46 Å | B=1-732 |
| 1JEY | X-ray | 2.5 Å | B=1-565 |
| 7ZYG | EM | 2.68 Å | B=1-732 |
| 1JEQ | X-ray | 2.7 Å | B=1-565 |
| 7ZVT | EM | 2.74 Å | B=1-732 |
| 6ERH | X-ray | 2.8 Å | B/D=2-555 |
| 7ZWA | EM | 2.8 Å | B=1-732 |
| 9CQ3 | EM | 2.8 Å | B/b=1-732 |
| 9GYF | EM | 2.8 Å | B=1-732 |
| 9N81 | EM | 2.8 Å | B/b=1-732 |
| 6ERG | X-ray | 2.9 Å | B/E=2-555 |
| 7Z87 | EM | 2.91 Å | C=1-732 |
| 9Q8X | EM | 2.94 Å | L/N=1-732 |
| 8ASC | X-ray | 2.95 Å | B/F/L/P=2-555 |
| 7SGL | EM | 3.0 Å | C=1-732 |
| 6ERF | X-ray | 3.01 Å | B/D/F/H=2-555 |
| 9CQ6 | EM | 3.1 Å | B/b=1-732 |
| 9N83 | EM | 3.1 Å | B/b=1-732 |
| 7AXZ | EM | 3.2 Å | B=1-732 |
Showing 20 of 62 experimental structures (best resolution first).
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