Abstract
Protein structure can be determined by either experimental method or by computational prediction, which commonly known as homology modelling. The objective of this study is to predict the structure of protein from Pseudomonas stutzeri using homology modelling. The suitable template was identified with 80.35% of sequence identity determined by sequence alignment. MODELLER was used to predict the model using the method of satisfaction of spatial restraints. The model was then analysed by computational analysis tools such as Ramachandran’s Plot, Errat, Verify3D Profile evaluation, Secondary Structure Prediction Analysis and Protein Binding Site (ProBiS). The results suggest that the model is reliable and has good stereochemical properties.
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