1EDT

CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H AT 1.9 ANGSTROMS RESOLUTION: ACTIVE SITE GEOMETRY AND SUBSTRATE RECOGNITION

1EDT の概要

• エントリーDOI: 10.2210/pdb1edt/pdb
• 分子名称: ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H, ENDO H (2 entities in total)
• 機能のキーワード: hydrolase (glucosidase)
• 由来する生物種: Streptomyces plicatus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29058.04

構造登録者

Van Roey, P.,Rao, V. (登録日: 1995-03-31, 公開日: 1995-08-04, 最終更新日: 2024-02-07)

主引用文献

Rao, V.,Guan, C.,Van Roey, P.
Crystal structure of endo-beta-N-acetylglucosaminidase H at 1.9 A resolution: active-site geometry and substrate recognition.
Structure, 3:449-457, 1995

PubMed Abstract: Endo-beta-N-acetylglucosaminidase H (Endo H), an endoglycosidase secreted by Streptomyces plicatus, hydrolyzes the glycosidic bond between the core N-acetyglucosamine residues of asparagine-linked high-mannose oligosaccharides. Endo H is a commonly used reagent in glycobiology research, including the characterization of oligosaccharides in glycoproteins. On-going crystallographic studies of Endo H and related endoglycosidases are aimed at identifying the molecular features that determine the different substrate specificities of these enzymes.

PubMed: 7663942
DOI: 10.1016/S0969-2126(01)00178-2

実験手法

X-RAY DIFFRACTION (1.9 Å)