3EWI
Structural analysis of the C-terminal domain of murine CMP-Sialic acid Synthetase
Summary for 3EWI
Entry DOI | 10.2210/pdb3ewi/pdb |
Related | 1QWJ |
Descriptor | N-acylneuraminate cytidylyltransferase (2 entities in total) |
Functional Keywords | beta barrel, had-like, rossmannoid fold, nucleotidyltransferase, nucleus, transferase |
Biological source | Mus Musculus (mouse) |
Cellular location | Nucleus : Q99KK2 |
Total number of polymer chains | 2 |
Total formula weight | 36744.59 |
Authors | Oschlies, M.,Dickmanns, A.,Stummeyer, K.,Gerardy-Schahn, R.,Ficner, R.,Muenster-Kuehnel, A.K. (deposition date: 2008-10-15, release date: 2009-08-18, Last modification date: 2023-12-27) |
Primary citation | Oschlies, M.,Dickmanns, A.,Haselhorst, T.,Schaper, W.,Stummeyer, K.,Tiralongo, J.,Weinhold, B.,Gerardy-Schahn, R.,von Itzstein, M.,Ficner, R.,Munster-Kuhnel, A.K. A C-terminal phosphatase module conserved in vertebrate CMP-sialic acid synthetases provides a tetramerization interface for the physiologically active enzyme. J.Mol.Biol., 393:83-97, 2009 Cited by PubMed: 19666032DOI: 10.1016/j.jmb.2009.08.003 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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