2BZB
NMR Solution Structure of a protein aspartic acid phosphate phosphatase from Bacillus Anthracis
Summary for 2BZB
Entry DOI | 10.2210/pdb2bzb/pdb |
NMR Information | BMRB: 7350 |
Descriptor | CONSERVED DOMAIN PROTEIN (1 entity in total) |
Functional Keywords | transferase, phosphatase, phosphorylation, sporulation, bacillus, anthracis, antithetical, negative, regulator, spine |
Biological source | BACILLUS ANTHRACIS |
Total number of polymer chains | 2 |
Total formula weight | 15031.75 |
Authors | Grenha, R.,Rzechorzek, N.J.,Brannigan, J.A.,Ab, E.,Folkers, G.E.,De Jong, R.N.,Diercks, T.,Wilkinson, A.J.,Kaptein, R.,Wilson, K.S. (deposition date: 2005-08-14, release date: 2006-09-25, Last modification date: 2024-05-15) |
Primary citation | Grenha, R.,Rzechorzek, N.J.,Brannigan, J.A.,de Jong, R.N.,Ab, E.,Diercks, T.,Truffault, V.,Ladds, J.C.,Fogg, M.J.,Bongiorni, C.,Perego, M.,Kaptein, R.,Wilson, K.S.,Folkers, G.E.,Wilkinson, A.J. Structural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli. J. Biol. Chem., 281:37993-38003, 2006 Cited by PubMed: 17001075DOI: 10.1074/jbc.M607617200 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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