Prediction of protein structures, functions and interactions using the IntFOLD7, MultiFOLD and ModFOLDdock servers

Nucleic Acids Res. 2023 Jul 5;51(W1):W274-W280. doi: 10.1093/nar/gkad297.


The IntFOLD server based at the University of Reading has been a leading method over the past decade in providing free access to accurate prediction of protein structures and functions. In a post-AlphaFold2 world, accurate models of tertiary structures are widely available for even more protein targets, so there has been a refocus in the prediction community towards the accurate modelling of protein-ligand interactions as well as modelling quaternary structure assemblies. In this paper, we describe the latest improvements to IntFOLD, which maintains its competitive structure prediction performance by including the latest deep learning methods while also integrating accurate model quality estimates and 3D models of protein-ligand interactions. Furthermore, we also introduce our two new server methods: MultiFOLD for accurately modelling both tertiary and quaternary structures, with performance which has been independently verified to outperform the standard AlphaFold2 methods, and ModFOLDdock, which provides world-leading quality estimates for quaternary structure models. The IntFOLD7, MultiFOLD and ModFOLDdock servers are available at:

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ligands
  • Models, Molecular
  • Protein Conformation
  • Protein Structure, Tertiary
  • Proteins* / chemistry
  • Software*


  • Ligands
  • Proteins