Published online 7 May 2015; doi:10.1038/nprot.2015.053 | Lawrence A Kelley1, Stefans Mezulis1, Christopher M Yates1,2, Mark N Wass1,2 & Michael J E Sternberg1
Phyre2 is a web-based platform designed to predict and analyze protein structure, function, and mutations. It provides a user-friendly interface for biologists to access advanced protein bioinformatics tools. Phyre2, an updated version of Phyre, uses advanced remote homology detection methods to build 3D models, predict ligand binding sites, and analyze the effects of amino acid variants. The platform guides users through the results with a simple interface, allowing them to interpret secondary and tertiary structures, domain composition, and model quality. Additional tools include finding protein structures in genomes, batch submission of sequences, and weekly searches for difficult-to-model proteins. Phyre2 is widely used, serving approximately 40,000 unique users annually and processing 700-1,000 submissions daily. While it excels in ease of use, it shares limitations with other structure prediction servers, such as the inability to model proteins with no detectable homology or to accurately predict the structural effects of point mutations. The platform is available at http://www.sbg.bio.ic.ac.uk/phyre2, and typical structure predictions are returned within 30 minutes to 2 hours after submission.Phyre2 is a web-based platform designed to predict and analyze protein structure, function, and mutations. It provides a user-friendly interface for biologists to access advanced protein bioinformatics tools. Phyre2, an updated version of Phyre, uses advanced remote homology detection methods to build 3D models, predict ligand binding sites, and analyze the effects of amino acid variants. The platform guides users through the results with a simple interface, allowing them to interpret secondary and tertiary structures, domain composition, and model quality. Additional tools include finding protein structures in genomes, batch submission of sequences, and weekly searches for difficult-to-model proteins. Phyre2 is widely used, serving approximately 40,000 unique users annually and processing 700-1,000 submissions daily. While it excels in ease of use, it shares limitations with other structure prediction servers, such as the inability to model proteins with no detectable homology or to accurately predict the structural effects of point mutations. The platform is available at http://www.sbg.bio.ic.ac.uk/phyre2, and typical structure predictions are returned within 30 minutes to 2 hours after submission.