Welcome! HADDOCK (High Ambiguity Driven
protein-protein DOCKing) is an information-driven flexible docking
approach for the modeling of biomolecular complexes.
HADDOCK distinguishes itself from ab-initio docking methods in the fact
that it encodes information from identified or predicted protein
interfaces in ambiguous interaction restraints (AIRs) to drive the docking
process. It also allows to define specific unambiguous distance restraints
(e.g. from MS cross-links) and supports a variety of other experimental
data including NMR residual dipolar couplings, pseudo contact shifts and
cryo-EM maps.
HADDOCK can deal with a large class of modeling problems including
protein-protein, protein-nucleic acids and protein-ligand complexes,
including multi-bodies (N>2) assemblies.
HADDOCK is one of the flagship software in the EU H2020
BioExcel Center of
Excellence for Biomolecular Research.
New to HADDOCK? To use the HADDOCK docking server you must have registered for an account.
Our server is easier than ever to use.
Try our new submission interface!
HADDOCK is used for excellent science and so far it has been
cited more than
5000 times!
Looking for support or questions about HADDOCK’s usage? Check our BioExcel forum!
Server information
feedback The access of HADDOCK
web server is free for non-profit users upon registration.
insert_chart Check our
usage statistics and
world map of users.
chevron_right The default
HADDOCK settings used by the server can be found
here.
chevron_right A list of
modified amino acids and another molecule types supported by HADDOCK
can be found
here.
chevron_right Currently running
HADDOCK v2.5-2024.03 - "A fresh spring version!"
Cite us:
If HADDOCK is useful for your work, please don't forget to cite us:
- R.V. Honorato, M.E. Trellet, B. Jiménez-García1, J.J. Schaarschmidt, M. Giulini, V. Reys, P.I. Koukos, J.P.G.L.M. Rodrigues, E. Karaca, G.C.P. van Zundert, J. Roel-Touris, C.W. van Noort, Z. Jandová, A.S.J. Melquiond and A.M.J.J. Bonvin. The HADDOCK2.4 web server: A leap forward in integrative modelling of biomolecular complexes. Nature Prot., In Press (2024).
- R.V. Honorato, P.I. Koukos, B. Jimenez-Garcia, A. Tsaregorodtsev, M. Verlato, A. Giachetti, A. Rosato and A.M.J.J. Bonvin (2021). "Structural biology in the clouds: The WeNMR-EOSC Ecosystem." Frontiers Mol. Biosci., 8, fmolb.2021.729513.
