TP53-binding protein 1 (TP53BP1) is a 1972-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q12888.
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The mean pLDDT of this model is 43.9 (very low 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 | 15% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 79% |
What pLDDT means and how to read it
Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs,…
Homooligomer (PubMed:16294047, PubMed:23345425, PubMed:23760478). Interacts with p53/TP53 (via the central domain) (PubMed:11877378, PubMed:12110597). Interacts with DCLRE1C (PubMed:15574327). Interacts with histone H2AX and this requires phosphorylation of H2AX on 'Ser-139' (PubMed:12607005). Interacts with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2) (PubMed:17190600). Has low…
Nucleus, Chromosome, Chromosome, centromere, kinetochore
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8SVI | X-ray | 1.15 Å | A=1484-1603 |
| 8SVH | X-ray | 1.16 Å | A=1484-1603 |
| 8SVG | X-ray | 1.21 Å | A=1484-1603 |
| 2G3R | X-ray | 1.25 Å | A=1484-1603 |
| 6VA5 | X-ray | 1.28 Å | A=1483-1606 |
| 6VIP | X-ray | 1.36 Å | A/B=1483-1606 |
| 7LIN | X-ray | 1.44 Å | B=1636-1650 |
| 3LGF | X-ray | 1.5 Å | A=1484-1603 |
| 4RG2 | X-ray | 1.5 Å | A/B=1483-1606 |
| 8SVJ | X-ray | 1.5 Å | A=1484-1603 |
| 8F0W | X-ray | 1.52 Å | A/B=1483-1606 |
| 3LGL | X-ray | 1.6 Å | A=1484-1603 |
| 8SWJ | X-ray | 1.6 Å | A/B/C/D=1483-1606 |
| 6MXY | X-ray | 1.62 Å | A/B=1484-1603 |
| 2IG0 | X-ray | 1.7 Å | A=1484-1603 |
| 6IUA | X-ray | 1.7 Å | B=1665-1686 |
| 8EOM | X-ray | 1.7 Å | A/B=1483-1606 |
| 8T2D | X-ray | 1.75 Å | A=1484-1603 |
| 5Z78 | X-ray | 1.76 Å | C=1484-1603 |
| 4X34 | X-ray | 1.8 Å | A/B=1484-1603 |
Showing 20 of 45 experimental structures (best resolution first).
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