PredUs: Prediction of Protein Interfaces Using Structural Alignment

PredUs is a method to predict protein-protein interfaces of a given monomeric query protein using its close and remote structural neighbors. Potential interfacial residues are identified by iteratively “mapping” interaction sites of each structural neighbor involved in a complex to individual residues in the query protein (see figure). Residues which frequently have interactions mapped to them are defined to be interfacial.

Please find a full description of the method can in References and information of using PredUs at the webserver Help page.

Start Webserver

Click here to launch PredUs.

How to use PredUs

Click here for help.


A full description of the method used in PredUs can be found in the following publications.

PredUs is based on an analysis of protein interface conservation:

Zhang QC, Petrey D, Norel R, Honig BH. Protein interface conservation across structure space. Proc Natl Acad Sci U S A. 2010 Jun 15;107(24):10896-901. Supplementary Information for the paper.

The PredUs web server was presented with improvements and more benchmarks:

Zhang QC, Deng L, Fisher M, Guan J, Honig B, Petrey D. PredUs: a web server for predicting protein interfaces using structural neighbors. Nucleic Acids Res. 2011;39:W283-W287.

For using PredUs interface prediction in our Markus function annotation server, please cite:

Fisher M, Zhang QC, Deng L, Dey F, Chen BY, Honig B, Petrey D. MarkUs: a server to navigate sequence–structure–function space. Nucleic Acids Res. 2011;39:W357-W361.


PredUs is supported by a funding from the NIH Grant # GM030518, NESG NIH Grant # GM074958 and MAGNet NIH Grant # CA121852.

Developed in the Honig Lab.


For questions about PreUs, contact