Pick protein and mutation

Predict stability effects of mutations on protein folding and interactions
First, input a protein ID such as Q9BUL8:
Protein input:
or upload PDB structure
Now, select a mutation:

Interactions affected by mutation:

, :
1
Warning: mutation is not in a domain
Warning: because the selected protein is not human, the calculations can take up to several hours.
Your email address (optional):
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Because ELASPIC uses structures of protein domains to predict stability/affinity effects, the mutation has to fall within domain boundries.
For more information about the mechanisms of ELASPIC, see the published paper.
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Final ΔΔG
The final Gibbs free energy change (ΔΔG) in kcal/mol is predicted using more than 70 sequential, molecular, and energetic features.
For more information see the original publication.
Seq iden:
Model score:
ELASPIC ΔΔG:
ELASPIC2 (EL2) score: