Tools · AlphaFold

AlphaFold explorer

Open any protein’s predicted structure from AlphaFold, check how confident the prediction is, and save figures for a paper or poster.

1 Choose a protein

Data load live from AlphaFold DB and UniProt (EMBL-EBI) in your browser. Nothing is contacted until you pick or search. What is shared

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Pick a protein above to open its dashboard.

↔ Compare two proteins

Fly and human cousins

Most human disease genes have a fly counterpart. Align two proteins, lay one AlphaFold model on top of the other and see how much of the shape has survived since their lineages split. Everything is computed on this device.

A not chosen

B not chosen

3 Try the API yourself

The same public endpoints this page uses. Send a request, inspect the answer, then copy the code into your own notebook.

Model metadata for one UniProt accession: confidence summary, sequence and links to the model, PAE and confidence files.

GET Enter a valid value to build the URL

Use it in your own code

import requests

r = requests.get("https://alphafold.ebi.ac.uk/api/prediction/P42212", timeout=30)
r.raise_for_status()
data = r.json()
entry = data[0]
print(entry["uniprotDescription"], "mean pLDDT", entry["globalMetricValue"])

Recipe: confidence table for any protein (Python)

# Per-residue confidence for P42212 from AlphaFold DB, saved as CSV
import csv, requests

acc = "P42212"
meta = requests.get(f"https://alphafold.ebi.ac.uk/api/prediction/{acc}", timeout=30).json()[0]
pdb = requests.get(meta["pdbUrl"], timeout=60).text

rows = [(int(l[22:26]), l[17:20], float(l[60:66]))           # residue number, name, pLDDT (B-factor)
        for l in pdb.splitlines() if l.startswith("ATOM") and l[12:16].strip() == "CA"]
with open(f"{acc}_plddt.csv", "w", newline="") as f:
    csv.writer(f).writerows([("residue", "name", "plddt"), *rows])

mean = sum(p for *_, p in rows) / len(rows)
print(f"{meta['uniprotDescription']}: {len(rows)} residues, mean pLDDT {mean:.1f}")

How to read it

  • pLDDT (0–100) is AlphaFold’s confidence for each residue. Above 90 is very confident; below 50 often marks a floppy, disordered region (Jumper et al. 2021; Ruff & Pappu 2021). Established: Replicated many times; textbook knowledge.
  • PAE shows how sure AlphaFold is about where two parts sit relative to each other. Dark blocks on the diagonal are domains; pale squares between them are flexible hinges.
  • Mutation scan: a protein language model (ESM-2) running on your device guesses which single changes the protein would tolerate (Lin et al. 2023). For human proteins it can be compared with AlphaMissense and reported variants (Cheng et al. 2023). Predictions only, never clinical advice.
  • Against experiment: lay a measured structure from the PDB over the prediction and see where they differ, residue by residue (TM-score; Zhang & Skolnick 2004).
  • Figures: every chart saves as editable SVG or 300/600 dpi PNG, and charts can be combined into one labelled figure. Methods and caveats for each chart are under “In detail”.
Methods and references (39)

References

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