DNA ligase 4 (LIG4) is a 911-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P49917.
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The mean pLDDT of this model is 88.2 (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 | 63% |
| 70 to 90 | Confident: backbone generally right | 28% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
DNA ligase involved in DNA non-homologous end joining (NHEJ); required for double-strand break (DSB) repair and V(D)J recombination (PubMed:12517771, PubMed:17290226, PubMed:23523427, PubMed:29980672, PubMed:33586762, PubMed:8798671, PubMed:9242410, PubMed:9809069). Catalyzes the NHEJ ligation step of the broken DNA during DSB repair by resealing the DNA breaks after the gap filling is completed (PubMed:12517771, PubMed:17290226, PubMed:9242410, PubMed:9809069). Joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction (PubMed:12517771, PubMed:17290226, PubMed:9242410, PubMed:9809069). LIG4 is mechanistically flexible: it can ligate nicks as well as…
Interacts with XRCC4; the LIG4-XRCC4 subcomplex has a 1:2 stoichiometry and XRCC4 is required for LIG4 stability (PubMed:10854421, PubMed:11702069, PubMed:12517771, PubMed:17290226, PubMed:19332554, PubMed:19837014, PubMed:21982441, PubMed:22658747, PubMed:24984242, PubMed:25934149, PubMed:9259561, PubMed:9809069, PubMed:17567543). Component of the core long-range non-homologous end joining…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4HTP | X-ray | 2.25 Å | A/B=1-240 |
| 1IK9 | X-ray | 2.3 Å | C=748-784 |
| 3II6 | X-ray | 2.4 Å | X/Y=654-911 |
| 3W1B | X-ray | 2.4 Å | A=1-609 |
| 6BKG | X-ray | 2.4 Å | A=1-620 |
| 3W1G | X-ray | 2.55 Å | A=1-609 |
| 7D9Y | X-ray | 2.76 Å | A=1-240 |
| 9CQ3 | EM | 2.8 Å | F/f=1-911 |
| 9N81 | EM | 2.8 Å | F/f=1-911 |
| 4HTO | X-ray | 2.81 Å | A=1-240 |
| 3W5O | X-ray | 2.84 Å | A/B=1-609 |
| 3VNN | X-ray | 2.9 Å | A=268-406 |
| 7D9K | X-ray | 2.9 Å | A=1-240 |
| 9CQ6 | EM | 3.1 Å | F/f=1-911 |
| 9N83 | EM | 3.1 Å | F/f=1-911 |
| 6BKF | X-ray | 3.25 Å | A=1-620 |
| 9N82 | EM | 3.3 Å | F/f=1-911 |
| 9CQC | EM | 3.4 Å | F/f=1-911 |
| 9IAX | EM | 3.97 Å | K=1-911 |
| 7NFC | EM | 4.14 Å | M/P=1-911 |
Showing 20 of 31 experimental structures (best resolution first).
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