1G97
S.PNEUMONIAE GLMU COMPLEXED WITH UDP-N-ACETYLGLUCOSAMINE AND MG2+
Summary for 1G97
Entry DOI | 10.2210/pdb1g97/pdb |
Related | 1G95 |
Descriptor | N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, MAGNESIUM ION, SODIUM ION, ... (5 entities in total) |
Functional Keywords | glmu, acetyltransferase, uridyltransferase, pyrophosphorylase, left-handed beta-sheet helix, trimer, magnesium, udp-n-acetylglucosamine, transferase |
Biological source | Streptococcus pneumoniae |
Cellular location | Cytoplasm: Q97R46 |
Total number of polymer chains | 1 |
Total formula weight | 50053.04 |
Authors | Kostrewa, D.,D'Arcy, A.,Kamber, M. (deposition date: 2000-11-22, release date: 2001-05-22, Last modification date: 2023-08-09) |
Primary citation | Kostrewa, D.,D'Arcy, A.,Takacs, B.,Kamber, M. Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution. J.Mol.Biol., 305:279-289, 2001 Cited by PubMed: 11124906DOI: 10.1006/jmbi.2000.4296 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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