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Protein Input using ONE of the following four options: [help]
Protein Symmetry (Optional):
  • Symmetry type: (e.g., C2 or C3 for Cyclic; D2 or D3 for Dihedral)
    Note: If the symmetry is not provided, the server will predict the symmetry type.
Docking Options:
  • Number of complex structures to generate:
  • Binding interface residue(s) (Optional):  Explanation
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  1. Yan Y, Wen Z, Wang X, Huang S-Y. Addressing recent docking challenges: A hybrid strategy to integrate template-based and free protein-protein docking. Proteins 2017;85:497-512.
  2. Huang S-Y, Zou X. An iterative knowledge-based scoring function for protein-protein recognition. Proteins 2008;72:557-579.
If you submit sequences, please also cite:
  1. Remmert M, Biegert A, Hauser A, Soing J. HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment. Nat Methods. 2011;9:173-175.
  2. W. R. Pearson and D. J. Lipman. Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 1988;85:2444-2448.
  3. Sievers F, Wilm A, Dineen D, Gibson TJ, Karplus K, Li W, Lopez R, McWilliam H, Remmert M, Soding J, Thompson JD, Higgins DG. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol Syst Biol. 2011;7:539.
  4. Marti-Renom MA, Stuart A, Fiser A, Sanchez R, Melo F, Sali A. Comparative protein structure modeling of genes and genomes. Annu Rev Biophys Biomol Struct 2000;29:291-325.
  5. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE. The Protein Data Bank. Nucleic Acids Res 2000;28:235-242.
The PDB database is updated monthly. Current version: 2018-06-02
huanglab@hust.edu.cn, Lab of Biophysics and Molecular Modeling