Abstract
In the present study we performed the comparative modeling, structural annotation, domain identification and the structural comparison of β-galactosidase enzyme from Aspergillus niger. Five domains were identified in the modeled structure at different residue regions. Two catalytic residues Glu200 and Glu298 were identified in the first domain of the modeled structure. The modeled structure showed highest similarity with crystal structure of Penicillium sp. β-galactosidase. The molecular docking of the structure with β-d-galactose was also performed. © 2013 Springer-Verlag Wien.
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Ghosh, S. K., Pandey, A., Arora, S., & Dwivedi, V. D. (2013). Comparative modeling and docking studies of β-galactosidase from Aspergillus niger. Network Modeling and Analysis in Health Informatics and Bioinformatics, 2(4), 297–302. https://doi.org/10.1007/s13721-013-0046-6
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