Motivation

Model quality assessment is a crucial part of protein structure prediction and a gateway to proper usage of models in biomedical applications. Many methods have been proposed for assessing the quality of structural models of protein monomers, but few methods for evaluating protein complex models. As protein complex structure prediction becomes a new challenge, there is an urgent need for model quality assessment methods that can accurately assess the accuracy of interface residues of complex structures.

Results

Here, we present DeepUMQA3, a web server for evaluating the accuracy of interface residues of protein complex structures using deep neural networks. For an input complex structure, features are extracted from three levels of overall complex, intra-monomer, and inter-monomer, and an improved deep residual neural network is used to predict per-residue lDDT and interface residue accuracy. DeepUMQA3 ranks first in the blind test of interface residue accuracy estimation in CASP15, with Pearson, Spearman, and AUC of 0.564, 0.535, and 0.755 under the lDDT measurement, which are 17.6%, 23.6%, and 10.9% higher than the second best method, respectively. DeepUMQA3 can also assess the accuracy of all residues in the entire complex and distinguish high- and low-precision residues.

Availability and implementation

The web sever of DeepUMQA3 are freely available at http://zhanglab-bioinf.com/DeepUMQA_server/.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.