4.7 Article Data Paper

The Metal-binding Protein Atlas (MbPA): An Integrated Database for Curating Metalloproteins in All Aspects

Journal

JOURNAL OF MOLECULAR BIOLOGY
Volume 435, Issue 14, Pages -

Publisher

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2023.168117

Keywords

metal-binding proteins; protein structures; diversity measure; mutation information

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MbPA is the most comprehensive resource for curating metal-binding proteins, containing a large amount of information on metal-binding proteins and species-specific proteins. Analysis of amino acid residue data at metal-binding sites shows that about 80% of metal ions tend to bind to cysteine, aspartic acid, glutamic acid, and histidine. In addition, MbPA includes 6855 potential pathogenic mutations related to metalloprotein. The resource is freely available.
Metal-binding proteins are essential for the vital activities and engage in their roles by acting in concert with metal cations. MbPA (The Metal-binding Protein Atlas) is the most comprehensive resource up to now dedicated to curating metal-binding proteins. Currently, it contains 106,373 entries and 440,187 sites related to 54 metals and 8169 species. Users can view all metal-binding proteins and species-specific proteins in MbPA. There are also metal-proteomics data that quantitatively describes protein expression in different tissues and organs. By analyzing the data of the amino acid residues at the metal-binding site, it is found that about 80% of the metal ions tend to bind to cysteine, aspartic acid, glutamic acid, and histidine. Moreover, we use Diversity Measure to confirm that the diversity of metal-binding is specific in different area of periodic table, and further elucidate the binding modes of 19 transition metals on 20 amino acids. In addition, MbPA also embraces 6855 potential pathogenic mutations related to metalloprotein. The resource is freely available at http://bioinfor.imu.edu.cn/mbpa. (c) 2023 Elsevier Ltd. All rights reserved.

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