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-Structure paper
Title | Allosteric regulation and substrate activation in cytosolic nucleotidase II from Legionella pneumophila. |
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Journal, issue, pages | Febs J., Vol. 281, Page 1613-1628, Year 2014 |
Publish date | Jul 18, 2012 (structure data deposition date) |
![]() | Srinivasan, B. / Forouhar, F. / Shukla, A. / Sampangi, C. / Kulkarni, S. / Abashidze, M. / Seetharaman, J. / Lew, S. / Mao, L. / Acton, T.B. ...Srinivasan, B. / Forouhar, F. / Shukla, A. / Sampangi, C. / Kulkarni, S. / Abashidze, M. / Seetharaman, J. / Lew, S. / Mao, L. / Acton, T.B. / Xiao, R. / Everett, J.K. / Montelione, G.T. / Tong, L. / Balaram, H. |
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Methods | X-ray diffraction |
Resolution | 2.53 - 2.7 Å |
Structure data | ![]() PDB-4g63: ![]() PDB-4ohf: |
Chemicals | ![]() ChemComp-PO4: ![]() ChemComp-HOH: ![]() ChemComp-5GP: ![]() ChemComp-MG: |
Source |
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![]() | DNA BINDING PROTEIN / Structural Genomics / PSI-Biology / Northeast Structural Genomics Consortium / NESG / alpha-beta protein / HAD-like superfamily / HYDROLASE / 3-domained structure that resembles HAD / nucleotidase. It catalyzes the breakdown of selected nucleoside monophosphates / cytosol |