Non-homologous end-joining factor 1 (NHEJ1) is a 299-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9H9Q4.
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The mean pLDDT of this model is 81.8 (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 | 65% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 19% |
What pLDDT means and how to read it
DNA repair protein involved in DNA non-homologous end joining (NHEJ); it is required for double-strand break (DSB) repair and V(D)J recombination and is also involved in telomere maintenance (PubMed:16439204, PubMed:16439205, PubMed:17317666, PubMed:17470781, PubMed:17717001, PubMed:18158905, PubMed:18644470, PubMed:20558749, PubMed:26100018, PubMed:28369633). Plays a key role in NHEJ by promoting the ligation of various mismatched and non-cohesive ends (PubMed:17470781, PubMed:17717001, PubMed:19056826). Together with PAXX, collaborates with DNA polymerase lambda (POLL) to promote joining of non-cohesive DNA ends (PubMed:25670504, PubMed:30250067). May act in concert with XRCC5-XRCC6 (Ku)…
Homodimer; mainly exists as a homodimer when not associated with XRCC4 (PubMed:18046455, PubMed:18158905, PubMed:25574025, PubMed:25670504, PubMed:25941166). Interacts with XRCC4; 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,…
Nucleus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2QM4 | X-ray | 2.3 Å | A/B/C/D=1-233 |
| 2R9A | X-ray | 2.5 Å | A/B=1-224 |
| 7ZYG | EM | 2.68 Å | F=1-299 |
| 6ERH | X-ray | 2.8 Å | M/T=281-299 |
| 9CQ3 | EM | 2.8 Å | C/c=1-299 |
| 9N81 | EM | 2.8 Å | C/c=1-299 |
| 6ERG | X-ray | 2.9 Å | C/F=287-299 |
| 9CQ6 | EM | 3.1 Å | C/c=1-299 |
| 9N83 | EM | 3.1 Å | C/c=1-299 |
| 9N82 | EM | 3.3 Å | C/c=1-299 |
| 9CQC | EM | 3.4 Å | C/c=1-299 |
| 9IOL | EM | 3.46 Å | M=287-299 |
| 3RWR | X-ray | 3.94 Å | D/E/H/I/L/M/O/Q/S/T/W/X=1-224 |
| 3SR2 | X-ray | 3.97 Å | C/D/G/H=1-224 |
| 9IAX | EM | 3.97 Å | D/M=1-299 |
| 7NFC | EM | 4.14 Å | Q/R=1-299 |
| 7NFE | EM | 4.29 Å | F/G=1-299 |
| 8EZA | EM | 4.39 Å | H/I=1-299 |
| 8BHV | EM | 4.51 Å | Q/R=1-299 |
| 7LT3 | EM | 4.6 Å | H/I=1-299 |
Showing 20 of 26 experimental structures (best resolution first).
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