2V0J

Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-acetylglucosamine-1-phosphate Uridyltransferase (GlmU)

2V0J の概要

• エントリーDOI: 10.2210/pdb2v0j/pdb
• 関連するPDBエントリー: 2V0H 2V0I 2V0K 2V0L
• 分子名称: BIFUNCTIONAL PROTEIN GLMU, 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: glmu, cell wall, magnesium, cell shape, transferase, peptidoglycan synthesis, associative mechanism, multifunctional enzyme, nucleotidyltransferase, uridylation, metal-binding, acyltransferase, catalytic mechanism
• 由来する生物種: HAEMOPHILUS INFLUENZAE
• 細胞内の位置: Cytoplasm (By similarity): P43889
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50791.82

構造登録者

Mochalkin, I.,Lightle, S.,Ohren, J.F.,Chirgadze, N.Y. (登録日: 2007-05-14, 公開日: 2008-01-15, 最終更新日: 2023-12-13)

• 主引用文献: Mochalkin, I.,Lightle, S.,Zhu, Y.,Ohren, J.F.,Spessard, C.,Chirgadze, N.Y.,Banotai, C.,Melnick, M.,Mcdowell, L.; Characterization of Substrate Binding and Catalysis in the Potential Antibacterial Target N-Acetylglucosamine-1-Phosphate Uridyltransferase (Glmu).; Protein Sci., 16:2657-, 2007; PubMed: 18029420; DOI: 10.1110/PS.073135107

実験手法

X-RAY DIFFRACTION (2 Å)