In silico analysis of Myoglobin in Channa striata |
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Authors: | Farzana Parveen Vineet Kumar Mishra |
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Institution: | Department of Biotechnology, Faculty of Science, Jamia Hamdard, New Delhi, India;┼Authors equally contributed |
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Abstract: | Myoglobin is a cytoplasmic hemoprotein, expressed solely in cardiac myocytes and oxidative skeletal muscle fibers, that reversibly
binds O2 by its heme residue. Myoglobin is an essential oxygen-storage hemoprotein capable of facilitating oxygen transport and
modulating nitric oxide homeostasis within cardiac and skeletal myocytes. Functionally, myoglobin is well accepted as an O2-
storage protein in muscle, capable of releasing O2 during periods of hypoxia or anoxia. There is no evidence available regarding
active sites, ligand binding sites, antigenic determinants and the ASA value of myoglobin in Channa striata. We further document
the predicted active sites in the structural model with solvent exposed ASA residues. During this study, the model was built by
CPH program and validated through PROCHECK, Verify 3D, ERRAT and ProSA for reliability. The active sites were predicted in
the model with further ASA analysis of active site residues. The discussed information thus provides the predicted active sites,
ligand binding sites, antigenic determinants and ASA values of myoglobin model in Channa striata. |
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Keywords: | Validation Active Sites Prediction Ligand Binding Sites Antigenic Determinants and ASA analysis |
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