1HM9
CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, GLMU, BOUND TO ACETYL COENZYME A AND UDP-N-ACETYLGLUCOSAMINE
Summary for 1HM9
Entry DOI | 10.2210/pdb1hm9/pdb |
Related | 1FWY 1FXJ 1HM0 1HM8 |
Descriptor | UDP-N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, CALCIUM ION, ACETYL COENZYME *A, ... (5 entities in total) |
Functional Keywords | acetyltransferase, bifunctional, drug design, pyrophosphorylase, rossmann-like fold, left-handed-beta-helix, trimer, domain-interchange, transferase |
Biological source | Streptococcus pneumoniae |
Total number of polymer chains | 2 |
Total formula weight | 104233.68 |
Authors | Sulzenbacher, G.,Gal, L.,Peneff, C.,Fassy, F.,Bourne, Y. (deposition date: 2000-12-05, release date: 2001-11-30, Last modification date: 2023-08-09) |
Primary citation | Sulzenbacher, G.,Gal, L.,Peneff, C.,Fassy, F.,Bourne, Y. Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture. J.Biol.Chem., 276:11844-11851, 2001 Cited by PubMed: 11118459DOI: 10.1074/jbc.M011225200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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