Protein structures are essential to understand the function. The predicted models have a broad range of the accuracy. Reliable estimates of the model quality are critical in determining the usefulness of the model to address a specific problem. In this study, a novel method has been presented to rank the models by their relative qualities. The proposed method first extracts various features from the three dimensional structures of proteins and then the learning-to-rank algorithm is used to rank the models based on their similarities with the native structures. Furthermore, a quasi single-model method is presented, which uses the top five identified models as references and ranks the other models by the average similarity with the reference models. Benchmark test is performed on a newly developed, template-based decoy generators which covers all the main structure classes of proteins. The proposed learning-to-rank method achieves an average Pearson correlation coefficient of 0.94 and a AUC value of 0.97, which consistently outperform all other well-developed methods. The quasi single-model can further improves the performance and achieve nearly perfect results with both PCC and AUC value of 0.99. The results demonstrate that the proposed method is an effective methodology for model quality assessment and provides the state-of-the-art performance.