4AC3

S.pneumoniae GlmU in complex with an antibacterial inhibitor

4AC3 の概要

• エントリーDOI: 10.2210/pdb4ac3/pdb
• 関連するPDBエントリー: 4AA7 4AAW
• 分子名称: BIFUNCTIONAL PROTEIN GLMU, N-{2,4-DIMETHOXY-5-[(2-PIPERIDIN-1-YLBENZYL)sulfamoyl]phenyl}acetamide, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: transferase, acetyl transferase, transferase-inhibitor complex
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• 細胞内の位置: Cytoplasm : Q8DQ18
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50025.08

構造登録者

Otterbein, L.,Breed, J.,Ogg, D.J. (登録日: 2011-12-12, 公開日: 2012-02-15, 最終更新日: 2023-12-20)

主引用文献

Green, O.M.,McKenzie, A.R.,Shapiro, A.B.,Otterbein, L.,Ni, H.,Patten, A.,Stokes, S.,Albert, R.,Kawatkar, S.,Breed, J.
Inhibitors of Acetyltransferase Domain of N-Acetylglucosamine-1-Phosphate-Uridyltransferase/ Glucosamine-1-Phosphate-Acetyltransferase (Glmu). Part 1: Hit to Lead Evaluation of a Novel Arylsulfonamide Series.
Bioorg.Med.Chem.Lett., 22:1510-, 2012

PubMed Abstract: A novel arylsulfonamide-containing series of compounds represented by 1, discovered by highthroughput screening, inhibit the acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). X-ray structure determination confirmed that inhibitor binds at the site occupied by acetyl-CoA, indicating that series is competitive with this substrate. This letter documents our early hit-to-lead evaluation of the chemical series and some of the findings that led to improvement in in-vitro potency against Gram-negative and Gram-positive bacterial isozymes, exemplified by compound 40.

PubMed: 22297115
DOI: 10.1016/J.BMCL.2012.01.016

実験手法

X-RAY DIFFRACTION (2.1 Å)