DNA damage-binding protein 1 (DDB1) is a 1140-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q16531.
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The mean pLDDT of this model is 92.0 (very high 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 | 78% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively (PubMed:14739464, PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16407252, PubMed:16482215, PubMed:16940174, PubMed:17079684, PubMed:25970626). Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruits proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP),…
Component of the UV-DDB complex which includes DDB1 and DDB2; the heterodimer dimerizes to give rise to a heterotetramer when bound to damaged DNA (PubMed:16223728, PubMed:16527807, PubMed:19109893, PubMed:22822215, PubMed:9632823). The UV-DDB complex interacts with monoubiquitinated histone H2A and binds to XPC via the DDB2 subunit (PubMed:16473935). Component of numerous DCX (DDB1-CUL4-X-box)…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9BBG | X-ray | 1.7 Å | A=1-1140 |
| 9EJQ | X-ray | 1.87 Å | A=1-1140 |
| 9BBI | X-ray | 1.9 Å | A=1-1140 |
| 9BZ0 | EM | 1.9 Å | d=1-1140 |
| 9BBE | X-ray | 2.0 Å | A=1-1140 |
| 9BBH | X-ray | 2.0 Å | A=1-1140 |
| 9FJX | X-ray | 2.0 Å | A=1-1140 |
| 9ZXN | X-ray | 2.07 Å | A=1-393, A=706-1140 |
| 9ZXM | X-ray | 2.19 Å | A=1-393, A=706-1140 |
| 8G46 | EM | 2.2 Å | A=1-395, A=706-1140 |
| 8ZSW | X-ray | 2.25 Å | A=1-1140 |
| 3EI3 | X-ray | 2.3 Å | A=1-1140 |
| 6UD7 | X-ray | 2.3 Å | B=1-395, B=706-1140 |
| 9SFM | X-ray | 2.39 Å | A=1-1140 |
| 3E0C | X-ray | 2.41 Å | A=1-1140 |
| 8TNQ | EM | 2.41 Å | A=1-395, A=706-1140 |
| 5FQD | X-ray | 2.45 Å | A/D=1-395, A/D=706-1140 |
| 8OIZ | X-ray | 2.5 Å | A=1-1140 |
| 8TNR | EM | 2.5 Å | A=1-395, A=706-1140 |
| 9OS2 | EM | 2.5 Å | A=1-1140 |
Showing 20 of 201 experimental structures (best resolution first).
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