Cellular tumor antigen p53 (TP53) is a 393-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04637.
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The mean pLDDT of this model is 75.1 (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 | 53% |
| 70 to 90 | Confident: backbone generally right | 7% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 30% |
What pLDDT means and how to read it
Multifunctional transcription factor that induces cell cycle arrest, DNA repair or apoptosis upon binding to its target DNA sequence (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:35618207, PubMed:36634798, PubMed:38653238, PubMed:9840937). Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17189187, PubMed:17317671,…
Forms homodimers and homotetramers (PubMed:19011621). Binds DNA as a homotetramer (PubMed:36108750). Interacts with AXIN1. Probably part of a complex consisting of TP53, HIPK2 and AXIN1 (By similarity). Interacts with histone acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and recruits them to promoters. Interacts (via C-terminus) with TAF1; when TAF1 is part of the TFIID…
Cytoplasm, Nucleus, Nucleus, PML body, Endoplasmic reticulum, Mitochondrion matrix, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9C5S | X-ray | 1.01 Å | A/B/C/D=17-30 |
| 3D06 | X-ray | 1.2 Å | A=94-293 |
| 5MHC | X-ray | 1.2 Å | P=382-393 |
| 8UQR | X-ray | 1.22 Å | A/B/C/D=326-356 |
| 6GGC | X-ray | 1.24 Å | A/B=94-312 |
| 6SHZ | X-ray | 1.24 Å | A/B=94-311 |
| 4MZI | X-ray | 1.25 Å | A=93-292 |
| 6GGE | X-ray | 1.25 Å | A/B=94-312 |
| 3LW1 | X-ray | 1.28 Å | P=385-393 |
| 5O1E | X-ray | 1.3 Å | A/B=94-312 |
| 6RL3 | X-ray | 1.3 Å | P=382-393 |
| 8E7A | X-ray | 1.3 Å | A=93-312 |
| 5O1C | X-ray | 1.32 Å | A/B=94-312 |
| 5O1H | X-ray | 1.32 Å | A/B=94-312 |
| 6GGB | X-ray | 1.32 Å | A/B=94-312 |
| 6GGF | X-ray | 1.32 Å | A/B=94-312 |
| 7B4N | X-ray | 1.32 Å | A=94-293 |
| 3ZME | X-ray | 1.35 Å | A/B=94-312 |
| 5AOK | X-ray | 1.35 Å | A/B=94-312 |
| 5G4N | X-ray | 1.35 Å | A/B=94-312 |
Showing 20 of 311 experimental structures (best resolution first).
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